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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

Modern Structural Chemistry.

TL;DR: Single-Crystal neutron diffraction is able to reveal a large amount of information related to molecular structure, which is not possible through single-crystal X-ray diffraction studies, and so provides significant enhancement to some X-Ray studies.
Proceedings ArticleDOI

Deep Learning of High-Order Interactions for Protein Interface Prediction

TL;DR: This work proposes to formulate the protein interface prediction as a 2D dense prediction problem, and proposes a novel deep model to incorporate the sequential information and high-order pairwise interactions to perform interface predictions.
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Structural Characterization of Backbone-Expanded Helices in Hybrid Peptides: (αγ)n and (αβ)n Sequences with Unconstrained β and γ Homologues of L-Val

TL;DR: Learning your I±I²I³'s: The diversity of hydrogen-bonding patterns in backbone-expanded hybrid helices is shown by crystal-structure determination of several oligomeric peptides.
Journal ArticleDOI

Dihedral-Based Segment Identification and Classification of Biopolymers I: Proteins

TL;DR: The DISICL algorithm is used to classify two databases of protein structures, jointly containing more than 10 million segments, and the analysis of polynucleotides is described and applied.
Journal ArticleDOI

Three Nimesulide Derivatives: Synthesis, Ab Initio Structure Determination from Powder X-ray Diffraction, and Quantitative Analysis of Molecular Surface Electrostatic Potential

TL;DR: In this paper, the crystal structures of nimesulide derivatives have been determined from laboratory powder X-ray diffraction data and the nature of intermolecular interactions in 2-4 has been analyzed through Hirshfeld surfaces and two-dimensional fingerprint plots.
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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