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Open AccessJournal ArticleDOI

The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain.

Linus Pauling, +2 more
- 01 Apr 1951 - 
- Vol. 37, Iss: 4, pp 205-211
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.

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Citations
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Journal ArticleDOI

Facile synthesis and chiral recognition of block and star copolymers containing stereoregular helical poly(phenyl isocyanide) and polyethylene glycol blocks

TL;DR: A new Pd(II) initiator bearing an alkyne headgroup was designed and synthesized, which initiated the living polymerization of phenyl isocyanide that lead to the formation of well-defined PPI with twoAlkyne groups on the same chain end.
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Tensile deformation and failure of North American porcupine quills

TL;DR: In this article, the fracture properties of porcupine quills were investigated at relative humidity of 65% and 100% and the fracture strength was found to be 146 ± MPa at 65% RH and 60 ± MPA at 100% RH.
Book ChapterDOI

Hair Structure, Function, and Physicochemical Properties

A. Franbourg, +1 more
TL;DR: Hair, the characteristic covering of mammalian skin, probably evolved from the epidermal scales of reptiles as discussed by the authors, and it is an important organ of touch and a part of normal sexual and physiological development.
Journal ArticleDOI

DNSS2: Improved ab initio protein secondary structure prediction using advanced deep learning architectures

TL;DR: Multiple advanced deep learning architectures (DNSS2) are developed to further improve secondary structure prediction of protein secondary structure and was systematically benchmarked on independent test data sets with eight state‐of‐art tools and consistently ranked as one of the best methods.
References
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Journal ArticleDOI

Two hydrogen-bonded spiral configurations of the polypeptide chain

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

The Structure of Fibrous Proteins.

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.
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