Mechanism of protein folding. III. Disulfide bonding.
It was shown in lysozyme and phospholipase, and generally in proteins with disulfide bonds, that after the formation of secondary structures the hydrophobic interactions between the key pairs responsible for folding tertiary structures bring several cysteine residues close together. Among the possible combination of cysteine residues some definite pairs are realized in the tertiary structure. In the Appendix to this paper an algebraic relation is given which must be satisfied for two cysteine residues to make a disulfide bond. This relation is too strict to be applied to real problems, where the two cysteines come close together, but the distance is still too great to yield a disulfide bond. In this case the two residues can attract each other by disulfide formation potential. A geometrical graphic representation is given for the locus of the H atom of the SH group in the cysteine residue. This looks like a lampshade and provides us with a guide to select the correct choice among cysteine pairs. This method is applied to lysozyme and phospholipase to supplement the discussion of the preceding paper (T. Yoshimura, H. Noguchi, T. Inoue and N. Saitô, Biophys. Chem. 40 (1991) 277).
Watanabe
K
K
Department of Applied Physics, Waseda University, Tokyo, Japan.
Nakamura
A
A
Fukuda
Y
Y
Saitô
N
N
D004220:Disulfides / Q000737:chemistry*; D004870:Erabutoxins / Q000737:chemistry; D009113:Muramidase / Q000737:chemistry; D010740:Phospholipases / Q000737:chemistry; D011487:Protein Conformation
D004220:Disulfides; D004870:Erabutoxins; D010740:Phospholipases; D009113:Muramidase