The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain.
TLDR
This work has used information about interatomic distances, bond angles, and other configurational parameters to construct two reasonable hydrogen-bonded helical configurations for the polypeptide chain; it is likely that these configurations constitute an important part of the structure of both fibrous and globular proteins, as well as of syntheticpolypeptides.Abstract:
During the past fifteen years we have been attacking the problem of the structure of proteins in several ways. One of these ways is the complete and accurate determination of the crystal structure of amino acids, peptides, and other simple substances related to proteins, in order that information about interatomic distances, bond angles, and other configurational parameters might be obtained that would permit the reliable prediction of reasonable configurations for the polypeptide chain. We have now used this information to construct two reasonable hydrogen-bonded helical configurations for the polypeptide chain; we think that it is likely that these configurations constitute an important part of the structure of both fibrous and globular proteins, as well as of synthetic polypeptides. A letter announcing their discovery was published last year [1].
The problem that we have set ourselves is that of finding all hydrogen-bonded structures for a single polypeptide chain, in which the residues are equivalent (except for the differences in the side chain R). An amino acid residue (other than glycine) has no symmetry elements. The general operation of conversion of one residue of a single chain into a second residue equivalent to the first is accordingly a rotation about an axis accompanied by translation along the axis. Hence the only configurations for a chain compatible with our postulate of equivalence of the residues are helical configurations. For rotational angle 180° the helical configurations may degenerate to a simple chain with all of the principal atoms, C, C' (the carbonyl carbon), N, and O, in the same plane.read more
Citations
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A supramolecular helix that disregards chirality
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Bundled assembly of helical nanostructures in polymeric micelles loaded with platinum drugs enhancing therapeutic efficiency against pancreatic tumor.
Yuki Mochida,Horacio Cabral,Yutaka Miura,Francesco Albertini,Shigeto Fukushima,Kensuke Osada,Kensuke Osada,Nobuhiro Nishiyama,Kazunori Kataoka +8 more
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The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat
Karin Kühnel,Thomas Jarchau,Eva Wolf,Ilme Schlichting,Ulrich Walter,Alfred Wittinghofer,Sergei V. Strelkov +6 more
TL;DR: The 1.3-A resolution crystal structure of the 45-residue-long tetramerization domain (TD) from human VASP is determined, which forms a right-handed alpha-helical coiled-coil structure with a similar degree of supercoiling as found in the widespread left-handed coiled coils with heptad repeats.
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Stereochemical punctuation marks in protein structures: glycine and proline containing helix stop signals
TL;DR: An analysis on the nature of alpha-helix stop signals has been carried out, using a dataset of 1057 helices identified from 250 high resolution, non-homologous, protein crystal structures, and reveals that Pro residues flanked by polar amino acids have a very strong tendency to terminate helices.
Journal ArticleDOI
Outcome of a Workshop on Applications of Protein Models in Biomedical Research
Torsten Schwede,Andrej Sali,Barry Honig,Michael Levitt,Helen M. Berman,David T. Jones,Steven E. Brenner,Stephen K. Burley,Rhiju Das,Nikolay V. Dokholyan,Roland L. Dunbrack,Krzysztof Fidelis,Andras Fiser,Adam Godzik,Yuanpeng J. Huang,Christine Humblet,Matthew P. Jacobson,Andrzej Joachimiak,Stanley R. Krystek,Tanja Kortemme,Andriy Kryshtafovych,Gaetano T. Montelione,John Moult,Diana Murray,Roberto Sanchez,Tobin R. Sosnick,Daron M. Standley,Terry R. Stouch,Sandor Vajda,Max Vasquez,John D. Westbrook,Ian A. Wilson +31 more
TL;DR: The proceedings and conclusions from the "Workshop on Applications of Protein Models in Biomedical Research" (the Workshop) that was held at the University of California, San Francisco on 11 and 12 July, 2008 are described.
References
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Journal ArticleDOI
Two hydrogen-bonded spiral configurations of the polypeptide chain
Linus Pauling,Robert B. Corey +1 more
TL;DR: In this article, two hydrogen-bonded spiral configurations of the polypeptide chain were constructed, with the residues all equivalent, except for variation in the side chain.
Journal ArticleDOI
Nature of the Intramolecular Fold in Alpha-Keratin and Alpha-Myosin
TL;DR: The normal folded configuration a, the extended configuration β, and the reversible intramolecular transformation from a-keratin (or a-myosin) to β-kerATin (or β-myOSin) is the basis of the remarkable long-range elastic properties of this group of protein fibres.