Dynamic and conformational switching in proteins.

Autor: Scheraga HA; Department of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, New York, USA., Rackovsky S; Department of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, New York, USA.; Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA.
Jazyk: angličtina
Zdroj: Biopolymers [Biopolymers] 2021 Oct; Vol. 112 (10), pp. e23411. Date of Electronic Publication: 2020 Dec 03.
DOI: 10.1002/bip.23411
Abstrakt: Using bioinformatic methods for treating protein dynamics, developed in earlier work, we study the relationship between sequence mobility and dynamics in proteins. It is shown that sequence mobility drives a transition between two dynamic regimes in proteins, and that the specific details of this transition differ qualitatively between α-helical proteins and those in other structural classes. We examine the possibility that conformational switching is related to dynamic switching, by considering a specific system of sequences which exhibit the switching phenomenon. It is shown that a relationship between dynamic and conformational switching is entirely plausible.
(© 2020 Wiley Periodicals LLC.)
Databáze: MEDLINE
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