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

Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications

TL;DR: A summary of the history, descriptions, principles, mechanisms, and applications of covalent labeling approaches in protein footprinting is presented, which combine to constitute a problem-solving toolbox that enables mass spectrometry as a valuable tool for HOS elucidation.
Journal ArticleDOI

Structure and Conformational Behavior of Biopolymers by Density Functional Calculations Employing Periodic Boundary Conditions. I. The Case of Polyglycine, Polyalanine, and Poly-α-aminoisobutyric Acid in Vacuo

TL;DR: Fully quantum mechanical calculations exploiting periodic boundary conditions (PBC) have been applied to the study of four different regular structures of the infinite polypeptides of glycine, alanine, and alpha-aminoisobutyric acid (Aib) in vacuo and reveal a remarkable dependence on the nature of the residue forming the polypePTides.
Journal ArticleDOI

General considerations on the structure of crystalline polyhydrocarbons

TL;DR: In this paper, the shape and mode of packing of macromolecules in the crystals of a crystal has been discussed, and some general principles leading to the determination of the shape of the crystal are discussed.
Journal ArticleDOI

Etude, par spectroscopie infra-rouge, de la conformation de quelques composés peptidiques modèles

TL;DR: In this paper, the N-H stretching bands in carbon tetrachloride were studied and it was found that there are two types of intramolecular hydrogen bonds in these molecules, which result in two different cyclized conformations, C5 and C7, containing respectively, five and seven atoms in the ring.
Journal ArticleDOI

Nickel-catalyzed transamidation of aliphatic amide derivatives

TL;DR: A two-step approach to achieve the transamidation of secondary aliphatic amides using non-precious metal catalysis and high-performance liquid chromatography is reported.
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)