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Ode (poem)
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Ode is a poem written by the English poet Arthur O'Shaughnessy and first published in 1873.[1] It is often referred to by its first line We are the music makers.
Wikisource has original text related to this article:
Ode (O'Shaughnessy)
The Ode is the first poem in O'Shaughnessy's collection Music and Moonlight (1874). It has nine stanzas, although it is commonly believed to be only three stanzas long. The opening stanza is:
We are the music makers,
And we are the dreamers of dreams,
Wandering by lone sea-breakers,
And sitting by desolate streams;—
World-losers and world-forsakers,
On whom the pale moon gleams:
Yet we are the movers and shakers
Of the world for ever, it seems.
The phrase "movers and shakers" (now almost universally misunderstood as a reference to powerful and worldly individuals and groups) originates here.
The poem has been set to music, or alluded to, many times: Sir Edward Elgar set the ode to music in 1912 in his work entitled The Music Makers, Op 69. The work was dedicated to Elgar's old friend Nicholas Kilburn and the first performance took place at the Birmingham Triennial Music Festival in 1912. Performances available include: The Music Makers, with Sir Adrian Boult conducting the London Philharmonic Orchestra in 1975 (reissued 1999), paired with Elgar's Dream of Gerontius; and the 2006 album Sea Pictures paired with The Music Makers, Simon Wright conducting the Bournemouth Symphony Orchestra. Zoltán Kodály (1882–1967) also set the ode to music in his work Music Makers, dedicated to Merton College, Oxford on the occasion of its 700th anniversary in 1964.
The Hungarian composer Zoltán Kodály also made a setting for and dedicated to Merton College, Oxford on the occasion of its 700th anniversary in 1964.
Cultural references and parodies[edit]
In the feature film Willy Wonka & the Chocolate Factory, after Willy Wonka (Gene Wilder) states that "The snozzberries taste like snozzberries!", Veruca Salt responds in an arrogant tone, "Snozzberries? Who ever heard of a snozzberry?" Willy Wonka grabs her cheeks, pulls her face towards him and gently replies, "We are the music makers, and we are the dreamers of dreams."
The line is played during the 89th Academy Awards In Memoriam section, when Gene Wilder is honored.
A sample of Willy Wonka's line appears at the beginning of Bassnectar's album Motions of Mutation.
Wonka's line is played at the beginning of Bastille's cover of "Dreams" by Fleetwood Mac.
The track "Nephatiti" from 808 State's album Ex:el uses a sample of Willy Wonka saying "We are the music makers, and we are the dreamers of dreams."
The introduction of the song "Nothing Less (Ft. Slug)" by the rap group Living Legends begins with the sample of Willy Wonka.
The track "Tighten Up" from The Specktator's album "About That Life" features an introduction of a sample of Willy Wonka saying "We are the music makers, and we are the dreamers of dreams." The same track on Spotify does not feature the same introduction.
The Aphex Twin track "We Are the Music Makers" from Selected Ambient Works 85-92 begins with a sample of Willy Wonka. It is repeated a number of times throughout the track.
Echolyn's 1992 song "A Little Nonsense" contains a sample of Wonka saying the phrase. The song's title also references another quote which Wonka sings, "A little nonsense now and then / Is relished by the wisest men."
The Gathering's instrumental song "Diamond Box" begins with a sample of Wonka's line.
The podcast The Music Makers begins with a sample of Wonka saying the phrase.
Scarling. has a song called "We Are the Music Makers." The line is said in the beginning of the chorus.
The first stanza is quoted in the animated TV show American Dad! on Season 5, Episode 6.
DJ Zinc's track "Music Makers" repeats this phrase throughout the song.
Joy Electric's 1996 album We Are the Music Makers is a reference to the first line.
The track "Movers And Shakers" by Eden Burning begins with a setting of the first stanza of "Ode."
The track "Music Makers" by ILS the track starts off with "We are the music makers, and we are the dreamers of dreams."
"Ode" is quoted at the end of the movie Last Summer in the Hamptons (1995).
The initial verse is used at the start of the Raymond E. Feist novel Rage of a Demon King.
In the Hollywood party scene in Stephen Sondheim's musical Merrily We Roll Along, the character Mary sardonically surveys the other guests and comments "These are the movers / These are the shapers / These are the people / That fill the papers."
The poem is used in the introduction of Elizabeth Haydon's book The Assassin King.
The opening line has been incorporated into the name of the New York band We Are the Music Makers, and the Singaporean Orchestra of the Music Makers.
The line “We are the music makers, we are the dreamers of dreams” is also quoted multiple times in the song “Imagineer” by Lange
The line “We are the music makers, we are the dreamers of dreams” was quoted in "Lonely Soul," a Chillout track by the musician Direct.
The line “We are the music makers, we are the dreamers of dreams” is quoted multiple times in the song “Dreamers of Dreams” by Orkidea
The line “We are the music makers, we are the dreamers of dreams” is quoted in the song “From Your Mind Into My Heart” by A Sol Mechanic
The line “We are the music makers, we are the dreamers of dreams” sentence was also used on track "East 98th Street" at Interstate Highway album Man with No Name (musician).
The line "We are the music makers, we are the dreamers of dreams" is quoted in the beginning of HugLife's trap remix of The Weeknd 's "Wicked Games"
The line “We are the music makers, we are the dreamers of dreams” is sampled on the track "Dreamers & Dreams" by Arctic Moon and Bryan Kearney
The line “We are the music makers, we are the dreamers of dreams” is used in the opening part of the song "Ode” by Sylence (Hardstyle Artist).
"Music Makers & Dreamers of Dreams" is a track off the album "As Above, So Below" by "Windmills".
The Seo Linn song "Music Makers", commissioned by RTÉ for the centenary of the 1916 Easter Rising, is in Irish but uses much of the first stanza of "Ode" as its chorus in English.
Three stanzas of the poem are referenced in "Black", a House track by Fabian Reichelt and Raycoux Jr. on the album Circle
South African band, Gimp, performed a rock anthem of the poem in 2005 at Woodstock South Africa
The phrase "We are the dreamers of dreams" is quoted in Episode 7 of the 9th Season of The Big Bang Theory.
The line "We are the music makers and We are the dreamers of dreams" is used in the Leander High School's Marching Band 2017 production "Internal Landscapes".
References[edit]
Jump up ^ O'Shaughnessy, Arthur (4 October 1873). "An Ode". Appleton's Journal. New York, NY: D. Appleton & Company. Retrieved 15 April 2014.
External links[edit]
Full Text of Poem
Retrieved from "https://en.wikipedia.org/w/index.php?title=Ode_(poem)&oldid=833643822"
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text:
Who Knows Where the Time Goes?
From Wikipedia, the free encyclopedia
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For other uses, see Who Knows Where the Time Goes? (disambiguation).
"Who Knows Where the Time Goes?"
Song by Sandy Denny
from the album Unhalfbricking (by Fairport Convention)
Released
1968
Songwriter(s)
Sandy Denny
Who Knows Where the Time Goes?
Excerpt from "Who Knows Where the Time Goes?" - 738 kb
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"Who Knows Where the Time Goes?" is a song written by the English folk-rock singer and songwriter Sandy Denny. Denny originally recorded the song as a demo in 1967, singing and playing guitar on the track. Later that year, she briefly joined the folk band The Strawbs, and re-recorded the song, again with only her voice and guitar, for what became the album All Our Own Work, which would not be released until 1973.
American folk singer Judy Collins heard a tape of the original demo recording in 1968, and decided to cover the song. She released her recording first as the B-side of her cover of "Both Sides, Now", and then as the title track of her album Who Knows Where the Time Goes, both released in 1968. Hers was the first widely available recording of the song.
In 1968 Denny joined the folk-rock band Fairport Convention. She recorded the song on her second album with the band, the 1969 album Unhalfbricking. This version had more of a rock influence.
"Who Knows Where the Time Goes?" became a signature song for both Denny and Fairport Convention, and has been covered by many artists.
In 2007, the Unhalfbricking version was voted "Favourite Folk Track Of All Time" by listeners of BBC Radio 2.[1]
Contents
[hide]
1 Structure
2 Cover versions
3 Soundtrack appearances
4 References
5 External links
Structure[edit]
The song is a slow-paced reflection in three verses on observed events ("Across the evening sky all the birds are leaving"[2][3]) Having described these observations, Denny then writes that for her, some things are timeless ("Before the winter's fire, I will still be dreamin'; I have no thought of time"[4]) and in the last line of the short chorus asks rhetorically "Who knows where the time goes?".
The song is in the key of E major and employs relatively complex jazz-like chord progressions.[4]
Cover versions[edit]
Cover versions have been recorded by, among others, Mia Doi Todd, 10,000 Maniacs, Mary Black, Eva Cassidy, Judy Collins, Nana Mouskouri, Lonnie Donegan, Nanci Griffith, Susanna Hoffs and Matthew Sweet, Deanna Kirk, Charlie Louvin, Cat Power, Eddi Reader, Julianne Regan (with Fairport Convention), Kate Rusby, Nina Simone (on her 1970 live album Black Gold), Barbara Dickson, Kate Wolf, Lumiere w/Sinéad O'Connor, Heather Masse (on the radio program A Prairie Home Companion),[5][6], Dez Mona.[7] and Itsuwa Mayumi
Besides Judy Collins' 1968 album Who Knows Where the Time Goes, Who Knows Where the Time Goes is the title of Fairport Convention's 1997 album, Michel Griffin's 2008 album[8], Kate Rusby's single CD, and Rondi Charleston's 2011 jazz album.
Soundtrack appearances[edit]
The Fairport Convention version was used as the closing music for the 2017 final episode of the Netflix series Grace and Frankie and the closing music in the 2009 film Don't Worry About Me. The Judy Collins version can be heard in the 1968 film The Subject Was Roses and the 1999 film A Walk on the Moon. The Nina Simone version is used in the 2002 film The Dancer Upstairs. In the 2011 Broadway production of Jerusalem by Jez Butterworth, the song is played in its entirety towards the end of the final act. A young girl puts an LP record on a turntable and the song plays as Mark Rylance's character, Johnny Byron, dances with her and is then brutally beaten by the girl's stepfather and his brothers. The version used is the live recording from BBC Radio Sounds of the Seventies, recorded September 11, 1973. The actress Lucy Hale sings it in an episode of the TV show Pretty Little Liars. The song was played in the BBC's Inspector George Gently episode "The Lost Child" set in 1968.
References[edit]
Jump up ^ "BBC - Press Office - Radio 2 Folk Awards 2007 winners". BBC. 6 February 2007. Retrieved 2008-08-07.
Jump up ^ "purple" is used in Denny's original home demo, later versions used "evening"
Jump up ^ "Sandy Denny". New Musical Express. Retrieved 2010-04-23.
^ Jump up to: a b "Who Knows Where The Time Goes Chords by Fairport Convention @ Ultimate-Guitar.Com". www.ultimate-guitar.com. Retrieved 2015-02-21.
Jump up ^ "Sandy Denny: Who Knows Where the Time Goes?". Reinhard Zierke. Retrieved 2017-06-02.
Jump up ^ "A Prairie Home Companion for December 31, 2011". American Public Media. 2012. Retrieved 27 January 2012.
Jump up ^ "Dez Mona - Persued Sinners (2010)". Retrieved 2016-12-26.
Jump up ^ http://www.michelgriffin.com/Album.php
External links[edit]
Lyrics of this song at MetroLyrics
[hide]
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t
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Solo albums
The North Star Grassman and the Ravens
Sandy
Like an Old Fashioned Waltz
Rendezvous
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Live albums
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It's Sandy Denny
Who Knows Where the Time Goes?
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Listen Listen - An Introduction to Sandy Denny
No More Sad Refrains: The Anthology
The Best of Sandy Denny (20th Century Masters: The Millennium Collection)
The Collection
A Boxful of Treasures
Where The Time Goes - Sandy '67
Live at the BBC
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The Music Weaver: Sandy Denny Remembered
Sandy Denny
The Notes and the Word: A Collection of Demos and Rarities
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Sandy Denny and the Strawbs
All Our Own Work: The Complete Sessions Remastered
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Fotheringay 2
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Rock On
Collaborations
Alex Campbell and His Friends
Sandy and Johnny (split album with Johnny Silvo)
Don't Stop Singing (Thea Gilmore)
Guest appearances
Led Zeppelin: "The Battle of Evermore"
The Who: Tommy
The Young Tradition: Galleries
Stefan Grossman: Ragtime Cowboy Jew
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Intrinsically disordered proteins
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Conformational flexibility in SUMO-1 protein (PDB:1a5r). The central part shows relatively ordered structure. Conversely, the N- and C-terminal regions (left and right, respectively) show ‘intrinsic disorder’, although a short helical region persists in the N-terminal tail. Ten alternative NMR models were morphed. Secondary structure elements: α-helices (red), β-strands (blue arrows). [1]
An intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure.[2][3][4] IDPs cover a spectrum of states from fully unstructured to partially structured and include random coils, (pre-)molten globules, and large multi-domain proteins connected by flexible linkers. They constitute one of the main types of protein (alongside globular, fibrous and membrane proteins).[5]
The discovery of IDPs has challenged the traditional protein structure paradigm, that protein function depends on a fixed three-dimensional structure. This dogma has been challenged over the 2000s and 2010s by increasing evidence from various branches of structural biology, suggesting that protein dynamics may be highly relevant for such systems. Despite their lack of stable structure, IDPs are a very large and functionally important class of proteins. In some cases, IDPs can adopt a fixed three-dimensional structure after binding to other macromolecules. Overall, IDPs are different from structured proteins in many ways and tend to have distinct properties in terms of function, structure, sequence, interactions, evolution and regulation.[6]
Contents
1 History
2 Biological roles
2.1 Flexible linkers
2.2 Linear motifs
2.3 Coupled folding and binding
2.4 Disorder in the bound state (fuzzy complexes)
3 Structural aspects
4 Experimental validation
5 Disorder prediction
5.1 Distinguishing IDPs from well-structured proteins
5.2 Prediction methods
6 Disorder and disease
7 Computer simulations
8 See also
9 References
10 External links
History[edit]
An ensemble of NMR structures of the Thylakoid soluble phosphoprotein TSP9, which shows a largely flexible protein chain.[7]
In the 1930s -1950s, the first protein structures were solved by protein crystallography. These early structures suggested that a fixed three-dimensional structure might be generally required to mediate biological functions of proteins. When stating that proteins have just one uniquely defined configuration, Mirsky and Pauling did not recognize that Fisher's work would have supported their thesis with his 'Lock and Key' model (1894). These publications solidified the central dogma of molecular biology in that the sequence determines the structure which, in turn, determines the function of proteins. In 1950, Karush wrote about 'Configurational Adaptability' contradicting all the assumptions and research in the 19th century. He was convinced that proteins have more than one configuration at the same energy level and can choose one when binding to other substrates. In the 1960s, Levinthal's paradox suggested that the systematic conformational search of a long polypeptide is unlikely to yield a single folded protein structure on biologically relevant timescales (i.e. seconds to minutes). Curiously, for many (small) proteins or protein domains, relatively rapid and efficient refolding can be observed in vitro. As stated in Anfinsen's Dogma from 1973, the fixed 3D structure of these proteins is uniquely encoded in its primary structure (the amino acid sequence), is kinetically accessible and stable under a range of (near) physiological conditions, and can therefore be considered as the native state of such "ordered" proteins.[citation needed]
During the subsequent decades, however, many large protein regions could not be assigned in x-ray datasets, indicating that they occupy multiple positions, which average out in electron density maps. The lack of fixed, unique positions relative to the crystal lattice suggested that these regions were "disordered". Nuclear magnetic resonance spectroscopy of proteins also demonstrated the presence of large flexible linkers and termini in many solved structural ensembles. It is now generally accepted that proteins exist as an ensemble of similar structures with some regions more constrained than others. Intrinsically Unstructured Proteins (IUPs) occupy the extreme end of this spectrum of flexibility, whereas IDPs also include proteins of considerable local structure tendency or flexible multidomain assemblies.These highly dynamic disordered regions of proteins have subsequently been linked to functionally important phenomena such as allosteric regulation and enzyme catalysis.[8][9]
In the 2000s, bioinformatic predictions of intrinsic disorder in proteins indicated that intrinsic disorder is more common in sequenced/predicted proteomes than in known structures in the protein database. Based on DISOPRED2 prediction, long (>30 residue) disordered segments occur in 2.0% of archaean, 4.2% of eubacterial and 33.0% of eukaryotic proteins.[10] In 2001, Dunker published his paper 'Intrinsically Disordered Proteins' questioning whether the newly found information was ignored for 50 years.[11]
In the 2010s it became clear that IDPs are highly abundant among disease-related proteins.[12]
Biological roles[edit]
Many disordered proteins have the binding affinity with their receptors regulated by post-translational modification, thus it has been proposed that the flexibility of disordered proteins facilitates the different conformational requirements for binding the modifying enzymes as well as their receptors.[13] Intrinsic disorder is particularly enriched in proteins implicated in cell signaling, transcription and chromatin remodeling functions.[14][15]
Flexible linkers[edit]
Disordered regions are often found as flexible linkers or loops connecting domains. Linker sequences vary greatly in length but are typically rich in polar uncharged amino acids. Flexible linkers allow the connecting domains to freely twist and rotate to recruit their binding partners via protein domain dynamics. They also allow their binding partners to induce larger scale conformational changes by long-range allostery.[8][2]
Linear motifs[edit]
Linear motifs are short disordered segments of proteins that mediate functional interactions with other proteins or other biomolecules (RNA, DNA, sugars etc.). Many roles of linear motifs are associated with cell regulation, for instance in control of cell shape, subcellular localisation of individual proteins and regulated protein turnover. Often, post-translational modifications such as phosphorylation tune the affinity (not rarely by several orders of magnitude) of individual linear motifs for specific interactions. Relatively rapid evolution and a relatively small number of structural restraints for establishing novel (low-affinity) interfaces make it particularly challenging to detect linear motifs but their widespread biological roles and the fact that many viruses mimick/hijack linear motifs to efficiently recode infected cells underlines the timely urgency of research on this very challenging and exciting topic. Unlike globular proteins IDPs do not have spatially-disposed active pockets. Nevertheless, in 80% of IDPs (~3 dozens) subjected to detailed structural characterization by NMR there are linear motifs termed PreSMos (pre-structured motifs) that are transient secondary structural elements primed for target recognition. In several cases it has been demonstrated that these transient structures become full and stable secondary structures, e.g., helices, upon target binding. Hence, PreSMos are the putative active sites in IDPs.[16]
Coupled folding and binding[edit]
Many unstructured proteins undergo transitions to more ordered states upon binding to their targets (e.g. Molecular Recognition Features (MoRFs)[17]). The coupled folding and binding may be local, involving only a few interacting residues, or it might involve an entire protein domain. It was recently shown that the coupled folding and binding allows the burial of a large surface area that would be possible only for fully structured proteins if they were much larger.[18] Moreover, certain disordered regions might serve as "molecular switches" in regulating certain biological function by switching to ordered conformation upon molecular recognition like small molecule-binding, DNA/RNA binding, ion interactions etc.[19]
The ability of disordered proteins to bind, and thus to exert a function, shows that stability is not a required condition. Many short functional sites, for example Short Linear Motifs are over-represented in disordered proteins.
Disorder in the bound state (fuzzy complexes)[edit]
Intrinsically disordered proteins can retain their conformational freedom even when they bind specifically to other proteins. The structural disorder in bound state can be static or dynamic. In fuzzy complexes structural multiplicity is required for function and the manipulation of the bound disordered region changes activity. The conformational ensemble of the complex is modulated via post-translational modifications or protein interactions.[20] Specificity of DNA binding proteins often depends on the length of fuzzy regions, which is varied by alternative splicing.[21]
Structural aspects[edit]
Intrinsically disordered proteins adapt many different structures in vivo according to the cell's conditions, creating a structural or conformational ensemble.[22][23]
Therefore, their structures are strongly function-related. However, only few proteins are fully disordered in their native state. Disorder is mostly found in intrinsically disordered regions (IDRs) within an otherwise well-structured protein. The term intrinsically disordered protein (IDP) therefore includes proteins that contain IDRs as well as fully disordered proteins.
The existence and kind of protein disorder is encoded in its amino acid sequence.[2] In general, IDPs are characterized by a low content of bulky hydrophobic amino acids and a high proportion of polar and charged amino acids, usually referred to as low hydrophobicity.[22] This property leads to good interactions with water. Furthermore, high net charges promote disorder because of electrostatic repulsion resulting from equally charged residues.[23] Thus disordered sequences cannot sufficiently bury a hydrophobic core to fold into stable globular proteins. In some cases, hydrophobic clusters in disordered sequences provide the clues for identifying the regions that undergo coupled folding and binding (refer to biological roles). Many disordered proteins reveal regions without any regular secondary structure These regions can be termed as flexible, compared to structured loops. While the latter are rigid and contain only one set of Ramachandran angles, IDPs involve multiple sets of angles.[23] The term flexibility is also used for well-structured proteins, but describes a different phenomenon in the context of disordered proteins. Flexibility in structured proteins is bound to an equilibrium state, while it is not so in IDPs.[23] Many disordered proteins also reveal low complexity sequences, i.e. sequences with over-representation of a few residues. While low complexity sequences are a strong indication of disorder, the reverse is not necessarily true, that is, not all disordered proteins have low complexity sequences. Disordered proteins have a low content of predicted secondary structure.
Experimental validation[edit]
Large-scale in-cell validation of IDR predictions is possible using biotin 'painting' [24].
Intrinsically unfolded proteins, once purified, can be identified by various experimental methods. The primary method to obtain information on disordered regions of a protein is NMR spectroscopy. The lack of electron density in X-ray crystallographic studies may also be a sign of disorder.
Folded proteins have a high density (partial specific volume of 0.72-0.74 mL/g) and commensurately small radius of gyration. Hence, unfolded proteins can be detected by methods that are sensitive to molecular size, density or hydrodynamic drag, such as size exclusion chromatography, analytical ultracentrifugation, small angle X-ray scattering (SAXS), and measurements of the diffusion constant. Unfolded proteins are also characterized by their lack of secondary structure, as assessed by far-UV (170-250 nm) circular dichroism (esp. a pronounced minimum at ~200 nm) or infrared spectroscopy. Unfolded proteins also have exposed backbone peptide groups exposed to solvent, so that they are readily cleaved by proteases, undergo rapid hydrogen-deuterium exchange and exhibit a small dispersion (<1 ppm) in their 1H amide chemical shifts as measured by NMR. (Folded proteins typically show dispersions as large as 5 ppm for the amide protons.) Recently, new methods including Fast parallel proteolysis (FASTpp) have been introduced, which allow to determine the fraction folded/disordered without the need for purification.[25][26] Even subtle differences in the stability of missense mutations, protein partner binding and (self)polymerisation-induced folding of (e.g.) coiled-coils can be detected using FASTpp as recently demonstrated using the tropomyosin-troponin protein interaction.[27] Fully unstructured protein regions can be experimentally validated by their hypersusceptibility to proteolysis using short digestion times and low protease concentrations.[28]

Bulk methods to study IDP structure and dynamics include SAXS for ensemble shape information, NMR for atomistic ensemble refinement, Fluorescence for visualising molecular interactions and conformational transitions, x-ray crystallography to highlight more mobile regions in otherwise rigid protein crystals, cryo-EM to reveal less fixed parts of proteins, light scattering to monitor size distributions of IDPs or their aggregation kinetics, Circular Dichroism to monitor secondary structure of IDPs.
Single-molecule methods to study IDPs include spFRET[29] to study conformational flexibility of IDPs and the kinetics of structural transitions, optical tweezers[30] for high-resolution insights into the ensembles of IDPs and their oligomers or aggregates, nanopores[31] to reveal global shape distributions of IDPs, magnetic tweezers[32] to study structural transitions for long times at low forces, high-speed AFM[33] to visualise the spatio-temporal flexibility of IDPs directly.
Disorder prediction[edit]
REMARK465 - missing electron densities in X-ray structure representing protein disorder (PDB: 1a22, human growth hormone bound to receptor). Compilation of screenshots from PDB database and molecule representation via VMD. Blue and red arrows point to missing residues on receptor and growth hormone, respectively.
Disorder prediction algorithms can predict Intrinsic Disorder (ID) propensity with high accuracy (approaching around 80%) based on primary sequence composition, similarity to unassigned segments in protein x-ray datasets, flexible regions in NMR studies and physico-chemical properties of amino acids.
Distinguishing IDPs from well-structured proteins[edit]
Separating disordered from ordered proteins is essential for disorder prediction. One of the first steps to find a factor that distinguishes IDPs from non-IDPs is to specify biases within the amino acid composition. The following hydrophilic, charged amino acids A, R, G, Q, S, P, E and K have been characterized as disorder-promoting amino acids, while order-promoting amino acids W, C, F, I, Y, V, L, and N are hydrophobic and uncharged. The remaining amino acids H, M, T and D are ambiguous, found in both ordered and unstructured regions.[2] This information is the basis of most sequence-based predictors. Regions with little to no secondary structure, also known as NORS (NO Regular Secondary structure) regions,[34] and low-complexity regions can easily be detected. However, not all disordered proteins contain such low complexity sequences.
Prediction methods[edit]
Main article: List of disorder prediction software
Determining disordered regions from biochemical methods is very costly and time-consuming. Due to the variable nature of IDPs, only certain aspects of their structure can be detected, so that a full characterization requires a large number of different methods and experiments. This further increases the expense of IDP determination. In order to overcome this obstacle, computer-based methods are created for predicting protein structure and function. It is one of the main goals of bioinformatics to derive knowledge by prediction. Predictors for IDP function are also being developed, but mainly use structural information such as linear motif sites.[4][35] There are different approaches for predicting IDP structure, such as neural networks or matrix calculations, based on different structural and/or biophysical properties.
Many computational methods exploit sequence information to predict whether a protein is disordered.[36] Notable examples of such software include IUPRED and Disopred. Different methods may use different definitions of disorder. Meta-predictors show a new concept, combining different primary predictors to create a more competent and exact predictor.
Due to the different approaches of predicting disordered proteins, estimating their relative accuracy is fairly difficult. For example, neural networks are often trained on different datasets. The disorder prediction category is a part of biannual CASP experiment that is designed to test methods according accuracy in finding regions with missing 3D structure (marked in PDB files as REMARK465, missing electron densities in X-ray structures).
Disorder and disease[edit]
Intrinsically unstructured proteins have been implicated in a number of diseases.[37] Aggregation of misfolded proteins is the cause of many synucleinopathies and toxicity as those proteins start binding to each other randomly and can lead to cancer or cardiovascular diseases. Thereby, misfolding can happen spontaneously because millions of copies of proteins are made during the lifetime of an organism. The aggregation of the intrinsically unstructured protein α-synuclein is thought to be responsible. The structural flexibility of this protein together with its susceptibility to modification in the cell leads to misfolding and aggregation. Genetics, oxidative and nitrative stress as well as mitochondrial impairment impact the structural flexibility of the unstructured α-synuclein protein and associated disease mechanisms.[38] Many key tumour suppressors have large intrinsically unstructured regions, for example p53 and BRCA1. These regions of the proteins are responsible for mediating many of their interactions. Taking the cell's native defense mechanisms as a model drugs can be developed, trying to block the place of noxious substrates and inhibiting them, and thus counteracting the disease.[39]
Computer simulations[edit]
Owing to high structural heterogeneity, NMR/SAXS experimental parameters obtained will be an average over a large number of highly diverse and disordered states (an ensemble of disordered states). Hence, to understand the structural implications of these experimental parameters, there is a necessity for accurate representation of these ensembles by computer simulations. All-atom molecular dynamic simulations can be used for this purpose but their use is limited by the accuracy of current force-fields in representing disordered proteins. Nevertheless, some force-fields have been explicitly developed for studying disordered proteins by optimising force-field parameters using available NMR data for disordered proteins. (examples are CHARMM 22*, CHARMM 32,[40] Amber ff03* etc.)
MD simulations restrained by experimental parameters (restrained-MD) have also been used to characterise disordered proteins.[41][42][43] In principle, one can sample the whole conformational space given an MD simulation (with accurate Force-field) is run long enough. Because of very high structural heterogeneity, the time scales that needs to be run for this purpose are very large and are limited by computational power. However, other computational techniques such as accelerated-MD simulations,[44] or replica exchange simulations[45][46], metadynamics[47][48] or methods using coarse-grained representation[49] have been used to sample broader conformational space in smaller time scales.
Moreover, various protocols and methods of analyzing IDPs, such as studies based on quantitative analysis of GC content in genes and their respective chromosomal bands, have been used to understand functional IDP segments.[50][51]
See also[edit]
IDPbyNMR
DisProt database
MobiDB database
Molten globule
Random coil
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External links[edit]
Intrinsically disordered protein at Proteopedia
MobiDB: a comprehensive database or intrinsic protein disorder annotations
IDEAL - Intrinsically Disordered proteins with Extensive Annotations and Literature
D2P2 Database of Disordered Protein Predictions
Gallery of images of intrinsically disordered proteins
First IDP journal covering all topics of IDP research
IDP Journal
Database of experimentally validated IDPs
IDP ensemble database
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Loi Krathong
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Loi Krathong
Floating krathong in Chiang Mai
Official name
Loi Krathong or Loy Krathong (ลอยกระทง)
Observed by
Thailand, Laos, northern Malaysia, Shan in Myanmar and Xishuangbanna in China,
Myanmar (as Tazaungdaing festival), Sri Lanka (as Il Poya), Cambodia (as Bon Om Touk)
Type
Asian
Date
Full moon of the 12th Thai month
2016 date
November 14
2017 date
November 3
2018 date
November 23
Frequency
annual
Related to
Tazaungdaing festival (in Myanmar), Il Poya (in Sri Lanka), Boita Bandana (in Odisha, India)[1] , Bon Om Touk (in Cambodia)
Loi Krathong[a] (Thai: ลอยกระทง, pronounced [lɔ̄ːj krā.tʰōŋ]) is a Siamese festival celebrated annually throughout southwestern Tai cultures (Thailand, Laos, Shan, Mon, Tanintharyi, Kelantan, Kedah and Xishuangbanna). The name could be translated as "to float a basket", and comes from the tradition of making krathong or buoyant, decorated baskets, which are then floated on a river.
Loi Krathong takes place on the evening of the full moon of the 12th month in the traditional Thai lunar calendar; hence, the exact date of the festival changes every year. In the Western calendar this usually falls in the month of November. In 2015 it was celebrated on November 25th; in 2016 it was celebrated on November 14th.
In Thailand, the festival is known as "Loi Krathong" (ลอยกระทง). Outside Thailand, this festival is celebrated under different names, including Myanmar as the "Tazaungdaing festival", Sri Lanka as "Il Full Moon Poya" and Cambodia as "Bon Om Touk".[2][3][4][5][6]
Contents
[hide]
1 Overview
1.1 Yi Peng
2 The aftermath
3 Gallery
4 See also
5 Notes
6 References
7 External links
Overview[edit]
A hand-made krathong, made from banana tree trunk and banana leaves, held together with pins, and decorated with flowers
Fireworks and large rafts on the Chao Phraya River, Loi Krathong Festival of Light, Bangkok, Nov 2004
According to the Royal Institute Dictionary 1999, loi (ลอย) means "to float", while krathong (กระทง) has various meanings, one of which is "a small container made of leaves which can be floated on water during the Loi Krathong festival".[7] Krathong is traditionally a small leaf container which is made to hold a small portion of goods like a traditional Thai dish (such as "Hor Mok") or dessert. The traditional krathong used for floating at the festival are made from a slice of a banana tree trunk or a spider lily plant. Modern krathongs are more often made of bread or Styrofoam. A bread krathong will disintegrate after a few days and can be eaten by fish. Banana stalk krathong are also biodegradable, but Styrofoam krathongs are sometimes banned, as they pollute the rivers and may take years to decompose. A krathong is decorated with elaborately-folded banana leaves, incense sticks, and a candle. A small coin is sometimes included as an offering to the river spirits.
On the night of the full moon, Thais launch their krathong on a river, canal or a pond, making a wish as they do so. The festival may originate from an ancient ritual paying respect to the water spirits.
Government offices, corporations, and other organizations launch large decorated krathongs. There are competitions for the best of these large krathongs. A beauty contest is a regular feature and fireworks have become common in recent years.
Loi Krathong is often claimed to have begun in the Sukhothai by a court lady named Nopphamat. However, it is now known that the Nopphamat tale comes from a poem written in the early Bangkok period.[8] According to King Rama IV, writing in 1863, it was a Brahmanical festival that was adapted by Thai Buddhists in Thailand to honor the Buddha, Prince Siddhartha Gautama. The candle venerates the Buddha with light, while the krathong's floating symbolizes letting go of all one's hatred, anger, and defilements. People sometimes cut their fingernails or hair and place the clippings on the krathong as a symbol of letting go of past transgressions and negative thoughts. Many Thais use the krathong to thank the Goddess of Water, the Hindu Goddess Ganga, Phra Mae Khongkha (Thai: พระแม่คงคา).
The beauty contests that accompany the festival are known as "Nopphamat Queen Contests". According to legend, Nang Nopphamat (Thai: นางนพมาศ; alternatively spelled as "Noppamas" or "Nopamas") was a consort of the 13th century Sukhothai king Sri Indraditya (who is also known as Phra Ruang) and she had been the first to float a decorated raft.[9] However, this is a new story which was invented during the first part of the 19th century. There is no evidence that a Nang Nopphamat ever existed. Instead, it is a matter of fact that a woman of this name was the leading character of a novel released at the end of the reign of King Rama III, around 1850 CE. Her character was written as guidance for all women who wished to become civil servants.
Kelantan in Malaysia celebrates Loi Krathong similarly, especially in the Tumpat area. The ministry in charge of tourism in Malaysia recognises it as an attraction for tourists. Many people visit the celebration each year.
Yi Peng[edit]
Thousands of Khom Loi in Mae Cho, Chiang Mai
Loi Krathong coincides with the Lanna (northern Thai) festival known as Yi Peng (Thai: ยี่เป็ง). Yi means "two" and peng means a "full moon day". Yi Peng refers to the full moon day in the second month according to the Lanna lunar calendar (the twelfth month of the Thai lunar calendar).[10] The festival is meant as a time to make merit (Thai: ทำบุญ; rtgs: tham bun).
Swarms of sky lanterns (Thai: โคมลอย; rtgs: khom loi), literally: 'floating lanterns', are launched into the air. Khom loi are made from a thin fabric, such as rice paper, stretched over a bamboo or wire frame, to which a candle or fuel cell is attached. When the fuel cell is lit, the resulting hot air is trapped inside the lantern and creates enough lift for the khom loi to float into the sky.
Because they are a hazard to passing aircraft and "...can cause damage to important places in the areas such as the Grand Palace [sic], temples and governmental offices,..." khom loi are increasingly subject to governmental restrictions. In Chiang Mai, authorities cancelled 78 flights in and out of Chiang Mai Airport on 3-4 November 2017. Another 79 flights were rescheduled.[11] In Bangkok, the public are prohibited from using fireworks and sky lanterns entirely. Violators may face three years imprisonment and/or a fine of 60,000 baht.[12] One hundred-ninety piers on the Chao Phraya River will be open to the public to float their krathongs.
During the festival, some people also decorate their houses, gardens, and temples with khom fai (Thai: โคมไฟ), intricately shaped paper lanterns which take on different forms. Khom thue (Thai: โคมถือ) are lanterns which are carried around hanging from a stick, khom khwaen (Thai: โคมแขวน) are the hanging lanterns, and khom pariwat (Thai: โคมปริวรรต), which are placed at temples and which revolve due to the heat of the candle inside. The most elaborate Yi Peng celebrations can be seen in Chiang Mai,[13] the ancient capital of the former Lanna kingdom, where now both Loi Krathong and Yi Peng are celebrated at the same time resulting in lights floating on the waters, lights hanging from trees/buildings or standing on walls, and lights floating in the sky. The tradition of Yi Peng was also adopted by certain parts of Laos during the 16th century.
The aftermath[edit]
In 2016, the Bangkok Metropolitan Administration (BMA) cleaned six tonnes of rubbish from the city's waterways on the day after Loi Krathong. The city governor said that 661,935 floats were collected from waterways across Bangkok. Of these, 617,901 (93.7 percent) were made of decomposible natural materials, while 44,034 were non-biodegradable Styrofoam floats. There were 163,679 fewer krathong collected than in 2015. The city mobilized 210 workers and 45 boats to collect floats from the Chao Phraya River and canals.[14]
In Nakhon Ratchasima, 50 workers collected krathong from the moat in the town centre near the Thao Suranaree Monument. In Buriram, more than 200 workers and volunteers in Mueang District cleared at least 20,000 krathong from the town's moat. There, Styrofoam krathong will be banned in 2017. In Lampang, more than 100 students and teachers from the Institute of Physical Education helped municipal workers clean up the Wang River in Mueang District.[14]
Gallery[edit]
Partially made krathong, showing trunk of banana tree and banana leaves.
Loi Krathong 2007, Lumpini Park, Bangkok
Loi Krathong 2007, Lumpini Park, Bangkok
Loi Krathong 2007, Lumpini Park, Bangkok
Launching khom loi, Yi Peng Festival, Mae Cho, Chiang Mai
Play media
Loi Krathong 2014
See also[edit]
Public holidays in Thailand
Thai folklore
Similar festivals
Tazaungdaing festival – Burmese equivalent of Loi Krathong
Bon Om Tuk - Cambodian equivalent of Loi Krathong
Diwali – Indian light festival
Tōrō nagashi – Japanese lantern festival
Bali Jatra
Leaf boat
Notes[edit]
Jump up ^ Alternative spellings include Loy Krathong, Loy Kratong, Loy Gratong, etc.
References[edit]
Jump up ^ https://m.facebook.com/story.php?story_fbid=1415855515180370&id=684563218309607&fs=5
Jump up ^ https://books.google.com.au/books?id=bNAJiwpmEo0C&printsec=frontcover#v=onepage&q&f=false
Jump up ^ http://calenworld.com/religion/buddhist-calendar
Jump up ^ http://www.telegraph.co.uk/news/2016/10/23/pictures-of-the-day-23-october-2016/the-tazaungdaing-festival-of-lights-celebrates-the-end-of-the-ra/
Jump up ^ http://srilankaembassy.com.pl/en/sri-lanka/national-festivals/il-poya/
Jump up ^ https://web.archive.org/web/20170201085505/http://www.accorhotels.com/gb/australia/magazine/one-hour-one-day-one-week/full-moon-festivals-8f5f4.shtml
Jump up ^ "พจนานุกรม ฉบับราชบัณฑิตยสถาน พ.ศ. 2542" [Royal Institute Dictionary 1999] (in Thai). Royal Institute of Thailand. 2007. Archived from the original on 2009-03-03. Retrieved 2014-06-06. Cite uses deprecated parameter |trans_title= (help)
Jump up ^ http://sconline.vru.ac.th/displayNews.php?id=65
Jump up ^ http://www.siamese-heritage.org/jsspdf/1951/JSS_038_2d_PhyaAnumanRajthon_LoiKratong.pdf Journal of the Siam Society, page 64
Jump up ^ สาระน่ารู้เกี่ยวกับประเพณียี่เป็งล้านนา [Info about Lanna's Yi Peng] (in Thai). Chiang Rai Provincial Culture Office. 2004. Retrieved 2014-06-06. Cite uses deprecated parameter |trans_title= (help)
Jump up ^ Atthakor, Ploenpote (1 November 2017). "Loy Krathong must be kept under control". Bangkok Post. Retrieved 1 November 2017.
Jump up ^ "Police and City Hall say no fireworks, firecrackers or sky lanterns on Loy Krathong Day". Thai PBS. 30 October 2017. Retrieved 31 October 2017.
Jump up ^ "Lantern Festival of the Yee Peng Month".
^ Jump up to: a b "City cleans 6 tonnes of krathong waste". Bangkok Post. 16 November 2016. Retrieved 16 November 2016.
External links[edit]
Wikimedia Commons has media related to Loi Krathong.
Sukhothai celebrations
Tourism Authority of Thailand (TAT) Loi Krathong Information
Suttinee Yavaprapas; Chaleo Manilerd; Thailand. Krasūang Watthanatham. External Relations Division; Thailand. Krasūang Watthanatham. Office of the Permanent Secretary (2004). Loy Krathong Festival. Ministry of Culture, External Relations Division. ISBN 978-974-9681-22-0. Retrieved 5 October 2011.
Donald K. Swearer (1 February 2010). The Buddhist world of Southeast Asia. SUNY Press. pp. 49–. ISBN 978-1-4384-3251-9. Retrieved 5 October 2011.
Anuman Rajadhon (Phrayā) (1956). Loy krathong & Songkran festival. National Culture Institute. Retrieved 5 October 2011.
The Kingdom of the Yellow Robe. Forgotten Books. pp. 358–367. ISBN 978-1-4400-9096-7. Retrieved 5 October 2011.
Retrieved from "https://en.wikipedia.org/w/index.php?title=Loi_Krathong&oldid=808729275"
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