Attenuating dependence on structural data in computing protein energy landscapes.

ABSTRACT:

Background

Nearly all cellular processes involve proteins structurally rearranging to accommodate molecular partners. The energy landscape underscores the inherent nature of proteins as dynamic molecules interconverting between structures with varying energies. In principle, reconstructing a protein's energy landscape holds the key to characterizing the structural dynamics and its regulation of protein function. In practice, the disparate spatio-temporal scales spanned by the slow dynamics challenge both wet and dry laboratories. However, the growing number of deposited structures for proteins central to human biology presents an opportunity to infer the relevant dynamics via exploitation of the information encoded in such structures about equilibrium dynamics.

Results

Recen

SUBMITTER: Morris D 

PROVIDER: S-EPMC6551245 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature