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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

Energetics of an n → π* Interaction that Impacts Protein Structure

TL;DR: The trans/cis ratio of the amide bond in N-formylproline phenylesters correlates with electron withdrawal by a para substituent, and an analogous interaction can stabilize the conformation of trans peptide bonds, alpha-helices, and polyproline type-II helices.
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Machine Learning Methods for Protein Structure Prediction

TL;DR: The development and application of hidden Markov models, neural networks, support vector machines, Bayesian methods, and clustering methods in 1-D, 2-D and 3-D protein structure predictions are reviewed.
Journal ArticleDOI

Natural protein fibers

TL;DR: The Extended Two-Phase Model (ETPM) has been developed and results in a detailed coverage of the bulk mechanical properties of α-helical fibers in terms of their known molecular and near-molecular structure.
Journal ArticleDOI

Protein 8‐class secondary structure prediction using conditional neural fields

TL;DR: This paper presents a new Probabilistic method for 8-class SS prediction using Conditional Neural Fields (CNFs), a recently-invented probabilistic graphical model that not only models complex relationship between sequence features and SS, but also exploits interdependency among SS types of adjacent residues.
Journal ArticleDOI

Infra-Red Dichroism and Protein Structure

R. D. B. Fraser, +1 more
- 20 Sep 1952 - 
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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