scispace - formally typeset
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.

read more

Citations
More filters
Journal ArticleDOI

Recurrent oligomers in proteins: An optimal scheme reconciling accurate and concise backbone representations in automated folding and design studies

TL;DR: In this paper, a knowledge-based strategy is introduced to carry out optimally automated subdivisions of protein fragments into classes of similarity, and the goal is to provide the minimal set of protein oligomers (called "oligons" for brevity) that is able to represent any other fragment.
Journal ArticleDOI

Cellulose and the role of hydrogen bonds: not in charge of everything

TL;DR: In the cellulose scientific community, hydrogen bonding is often used as the explanation for a large variety of phenomena and properties related to cellulose and cellulose-based materials as mentioned in this paper.
Journal ArticleDOI

Characterization of antimicrobial activity and mechanisms of low amphipathic peptides with different α-helical propensity.

TL;DR: A series of imperfect amphipathic peptides designed by placing different types of amino acid residues at the hydrogen bond linked positions of α-helix structures to characterize their antimicrobial properties and mechanism of action exhibited excellent antimicrobial potency.
Journal ArticleDOI

Characterization at atomic resolution of peptide helical structures.

TL;DR: A survey of literature for the various types of helices experimentally observed in highresolution single crystal x‐ray diffraction analyses of peptides has allowed to determine accurate conformational and helical parameters for theVarious secondary structures such as the α‐helix, the 310‐helik, the fully extended conformation (25‐helIX) and the β‐bend ribbon spiral.
Journal ArticleDOI

Energetics of protein hydrogen bonds.

TL;DR: In this issue, an article gives insight into the microenvironment's influence on the contribution of hydrogen bonds to protein stability.
References
More filters
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.
Related Papers (5)