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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

Ambidextrous molecules: cylindrical peptide structures formed by fusing left- and right-handed helices.

TL;DR: The structural characterization of a 14-residue hydrophobic peptide containing two heptapeptide blocks of opposite chirality is described, enabling peptides with strong helix-forming tendencies generated so as to fuse left- and right-handed cylindrical screws in the same molecule.
Journal ArticleDOI

Three-Dimensional Chemical Mapping of a Single Protein in the Hydrated State with Atom Probe Tomography.

TL;DR: The quantitative distribution and proportion of iron isotopes from a single ferritin core have been determined for the first time, as well as identification of the possible sites of amino acids inside the protein shell.
Journal ArticleDOI

Increasing protein stability by engineering the n → π* interaction at the β-turn

TL;DR: It is demonstrated that an n → π* interaction increases the structural stability of proteins by restricting the ϕ torsion angle and the results suggest that amino acid side-chain identity and its rotameric conformation play an important and decisive role in dictating the strength of an n→π* interaction.
Journal ArticleDOI

Chemie und Aufbau der Wolle

TL;DR: Wool is a fibrous biomaterial with an exceptional multicellular structure and complex chemical composition as mentioned in this paper, which is shown for some selected topics in this paper. But this paper is not a comprehensive review of the literature.
Journal ArticleDOI

α-Configuration of Fibrous Proteins

R.D.B. Fraser, +1 more
- 01 Feb 1961 - 
TL;DR: Detailed calculations by Crick5 and Lang6 showed that a group of three such helices twisted about a common axis to form a rope gives a satisfactory agreement with the observed diffraction pattern in the 1.2 and 1.5 Å.
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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