Experimentally Derived and Computationally Optimized Backbone Conformational Statistics for Blocked Amino Acids.

ABSTRACT: Experimentally derived, amino acid specific backbone dihedral angle distributions are invaluable for modeling data-driven conformational equilibria of proteins and for enabling quantitative assessments of the accuracies of molecular mechanics force fields. The protein coil library that is extracted from analysis of high-resolution structures of proteins has served as a useful proxy for quantifying intrinsic and context-dependent conformational distributions of amino acids. However, data that go into coil libraries will have hidden biases, and ad hoc procedures must be used to remove these biases. Here, we combine high-resolution biased information from protein structural databases with unbiased low-resolution information from spectroscopic measurements of blocked amino acids to obtain expe

SUBMITTER: Choi JM 

PROVIDER: S-EPMC10846683 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature