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Isopeptide Crosslinks—Their Occurrence and Importance in Protein Structure
Author(s) -
Asquith R. S.,
Otterburn M. S.,
Sinclair W. J.
Publication year - 1974
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.197405141
Subject(s) - globular protein , lysine , covalent bond , chemistry , fibrinogen , side chain , fibrin , aspartic acid , glutamic acid , biochemistry , amino acid , polymer chemistry , combinatorial chemistry , polymer , organic chemistry , biology , immunology
Isopeptide links refer to bonds between the ϵ‐amino group of lysine and the side‐chain carboxyl groups of glutamic or aspartic acid. Covalent crosslinks of this kind, which undoubtedly occur in protein feedstuffs and reduce their nutritional value, also participate In the fibrinogen → fibrin transformation and play a part in stabilizing the structure of keratins. Isopeptide links also arise on heating of both fibrous and globular proteins, the amount formed depending upon the severity of heat treatment. The mode of formation and the significance of these crosslinks require further elucidation.