TOPOLOGICAL FEATURES OF PROTEIN STRUCTURES - KNOTS AND LINKS

Authors
Citation
Cz. Liang et K. Mislow, TOPOLOGICAL FEATURES OF PROTEIN STRUCTURES - KNOTS AND LINKS, Journal of the American Chemical Society, 117(15), 1995, pp. 4201-4213
Citations number
100
Categorie Soggetti
Chemistry
ISSN journal
00027863
Volume
117
Issue
15
Year of publication
1995
Pages
4201 - 4213
Database
ISI
SICI code
0002-7863(1995)117:15<4201:TFOPS->2.0.ZU;2-T
Abstract
A survey of the Brookhaven Protein Data Bank has revealed the presence of catenated closed loops (topological links) in the structures of qu inoprotein methylamine dehydrogenase, cytochrome, and human chorionic gonadotropin, and of knotted and catenated closed loops in ascorbate o xidase and human lactoferrin. All of these structures are topologicall y chiral. In contrast to polynucleotide knots and links in circular DN A, which are constructed entirely from the backbone polynucleotide cha in, knots and links in proteins are formed from polypeptide chain segm ents combined with intrachain cross-links (cofactors and/or cystine di sulfide bridges) that are thermodynamically but not kinetically stable . The question of whether bonds other than covalent ones are suitable for inclusion in the molecular graph of a protein is critically discus sed.