Structural Rigidity and Protein Thermostability in Variants of Lipase A from Bacillus subtilis.

ABSTRACT: Understanding the origin of thermostability is of fundamental importance in protein biochemistry. Opposing views on increased or decreased structural rigidity of the folded state have been put forward in this context. They have been related to differences in the temporal resolution of experiments and computations that probe atomic mobility. Here, we find a significant (p = 0.004) and fair (R2 = 0.46) correlation between the structural rigidity of a well-characterized set of 16 mutants of lipase A from Bacillus subtilis (BsLipA) and their thermodynamic thermostability. We apply the rigidity theory-based Constraint Network Analysis (CNA) approach, analyzing directly and in a time-independent manner the statics of the BsLipA mutants. We carefully validate the CNA results on macroscopic and mi

SUBMITTER: Rathi PC 

PROVIDER: S-EPMC4493141 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature