UNEXPECTED DIFFERENT DISULFIDE CONNECTIVITIES OF CYSTEINE-RICH PEPTIDES WITH IDENTICAL CYSTEINE PATTERNS

摘要

Synthetic cysteine-rich replicates of naturally occurring peptides such as hormones, neurotransmitters, enzyme inhibitors, defensins and toxins often can be oxidatively folded in high yields to their native structures. The presence of identical cysteine patterns in the sequence generally leads to identical disulfide connectivities and homologous spatial structures despite significant variability in the non-cysteine positions. The consensus evolved to attribute unknown disulfide connectivities on the homology basis of cysteine patterns.