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
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.