Predicting the melting point of human C-type lysozyme mutants.

ABSTRACT: A complete understanding of the relationships between protein structure and stability remains an open problem. Much of our insight comes from laborious experimental analyses that perturb structure via directed mutation. The glycolytic enzyme lysozyme is among the most well characterized proteins under this paradigm, due to its abundance and ease of manipulation. To speed up such analyses, efficient computational models that can accurately predict mutation effects are needed. We employ a minimal Distance Constraint Model (mDCM) to predict the stability of a series of lysozyme mutants (specifically, human wild-type C-type lysozyme and 14 point mutations). With three phenomenological parameters that characterize microscopic interactions, the mDCM parameters are determined by obtaining the lea

SUBMITTER: Verma D 

PROVIDER: S-EPMC4667962 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature