Involvement of Local, Rapid Conformational Dynamics in Binding of Flexible Recognition Motifs.

ABSTRACT: Flexible protein sequences populate ensembles of rapidly interconverting states differentiated by small-scale fluctuations; however, elucidating whether and how the ensembles determine function experimentally is challenged by the combined high spatial and temporal resolution needed to capture the states. We used carbon-deuterium (C-D) bond vibrations incorporated as infrared probes to characterize with residue-specific detail the heterogeneity of states adopted by proline-rich (PR) sequences and assess their involvement in recognition of Src homology 3 domains. The C-D absorption envelopes provided evidence for two or three sub-populations at all proline residues. The changes in the subpopulations induced by binding generally reflected recognition by conformational selection but depended o

SUBMITTER: Bukowski GS 

PROVIDER: S-EPMC8066399 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature