Composition-dependent energetic contribution of complex salt bridges to collagen stability.

ABSTRACT: Complex salt bridges, on which three or more charged residues interplay simultaneously, cannot be considered as addition of individual salt bridges. This is still an intriguing problem in protein folding and stability. Here, we used an obligated ABC-type collagen heterotrimer as a platform to study the relationship between energetic contributions and conformational details of three-body complex salt bridges anchored by positively charged residues, K and R. Eight complex salt bridges were constructed by engineering point mutations in the heterotrimer. The circular dichroism measurements showed that the K-anchored complex salt bridges were stronger than the R-anchored ones. The molecular dynamics simulation revealed that both types of salt bridges had distinct dynamic features. The energetic

SUBMITTER: Sun T 

PROVIDER: S-EPMC8391061 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature