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Topological considerations in protein structure. I. Disulfide linkage
Author(s) -
Kato Ikunoshin,
Narita Kozo,
Fuke Ichita
Publication year - 1966
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1966.360040704
Subject(s) - chemistry , disulfide bond , disulfide linkage , cystine , linkage (software) , topology (electrical circuits) , crystallography , biochemistry , gene , combinatorics , cysteine , mathematics , enzyme
The patterns of disulfide bridges in proteins were considered by using the concept of topological information content. It was proposed that the difference between topological informal ion content in the half‐cystine residues of the native state and of the fully reduced form of a protein is related to the problems of the renaturation of the fully reduced and denatured protein. Specifically, when there is no difference between the topological information contents of the two states, the reduced protein is able to recover its native conformation. The concept reported in the present paper is consistent without exception with reported experimental results.