Using steered molecular dynamic tension for assessing quality of computational protein structure models.

ABSTRACT: The native structures of proteins, except for notable exceptions of intrinsically disordered proteins, in general take their most stable conformation in the physiological condition to maintain their structural framework so that their biological function can be properly carried out. Experimentally, the stability of a protein can be measured by several means, among which the pulling experiment using the atomic force microscope (AFM) stands as a unique method. AFM directly measures the resistance from unfolding, which can be quantified from the observed force-extension profile. It has been shown that key features observed in an AFM pulling experiment can be well reproduced by computational molecular dynamics simulations. Here, we applied computational pulling for estimating the accuracy of co

SUBMITTER: Monroe L 

PROVIDER: S-EPMC9133218 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature