Accurate protein structure prediction with hydroxyl radical protein footprinting data.

ABSTRACT: Hydroxyl radical protein footprinting (HRPF) in combination with mass spectrometry reveals the relative solvent exposure of labeled residues within a protein, thereby providing insight into protein tertiary structure. HRPF labels nineteen residues with varying degrees of reliability and reactivity. Here, we are presenting a dynamics-driven HRPF-guided algorithm for protein structure prediction. In a benchmark test of our algorithm, usage of the dynamics data in a score term resulted in notable improvement of the root-mean-square deviations of the lowest-scoring ab initio models and improved the funnel-like metric P_near for all benchmark proteins. We identified models with accurate atomic detail for three of the four benchmark proteins. This work suggests that HRPF data along wit

SUBMITTER: Biehn SE 

PROVIDER: S-EPMC7804018 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature