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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

Handedness preference and switching of peptide helices. Part II: Helices based on noncoded α-amino acids

TL;DR: Experimental and theoretical data is presented on handedness preference and switches between right‐handed and left‐handed helical peptide structures generated by protein amino acids or appropriately designed, side‐chain modified analogs, and three categories of screw‐sense issues.
Journal ArticleDOI

Investigation on mechanisms of glycopeptide nanoparticles for drug delivery across the blood-brain barrier.

TL;DR: Evidence suggested that g7-NP BBB crossing is enabled by multiple pathways, mainly membrane-membrane interaction and macropinocytosis-like mechanisms.
Journal ArticleDOI

[The structure of L-poly-gamma-benzyl glutamate in solution. Configuration of a helix different from helix alpha and transitions between helical forms].

TL;DR: The structure of poly- γ -benzyl-L -glutamate (PLBG) in solution in dimethyl-formamide, pyridine and m-cresol has been studied by X-ray diffraction techniques as discussed by the authors.
Journal ArticleDOI

Adding backbone to protein folding: why proteins are polypeptides

TL;DR: It is argued that the chemical nature of the polypeptide backbone is the central determinant of the three-dimensional structures of proteins and 'Sidechain-only' models, based on hydrophobicity patterns, fail to account for the properties of the backbone and thus will have difficulty capturing essential features of a folding pathway.
Journal ArticleDOI

Dimensional Change of Polypeptide Molecules in the Helix‐Coil Transition Region. II

TL;DR: In this paper, the mean square end-to-end distance and radius of gyration for polypeptide molecules in the helix-coil transition region were calculated for illustration.
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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