Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy

O'Brien, Evan S.; Fuglestad, Brian; Lessen, Henry J.; Stetz, Matthew A.; Lin, Danny W.; Marques, Bryan S.; Gupta, Kushol; Fleming, Karen G.; Wand, A. Joshua

doi:10.1002/ange.202003527

Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy

Journal Article · Thu Apr 30 00:00:00 EDT 2020 · Angewandte Chemie

DOI:https://doi.org/10.1002/ange.202003527· OSTI ID:1632011

^[1]; Fuglestad, Brian ^[2]; Lessen, Henry J. ^[3]; Stetz, Matthew A. ^[1]; Lin, Danny W. ^[1]; Marques, Bryan S. ^[1]; Gupta, Kushol ^[1]; Fleming, Karen G. ^[3]; ^[4]

Department of Biochemistry &, Biophysics University of Pennsylvania Perelman School of Medicine Philadelphia PA 19104 USA
Department of Biochemistry &, Biophysics University of Pennsylvania Perelman School of Medicine Philadelphia PA 19104 USA, Present address: Department of Chemistry Virginia Commonwealth University Richmond VA 23284 USA
Department of Biophysics Johns Hopkins University Baltimore MD 21218 USA
Department of Biochemistry &, Biophysics Texas A&,M University College Station TX 77843 USA, Department of Biochemistry &, Biophysics University of Pennsylvania Perelman School of Medicine Philadelphia PA 19104 USA

Abstract

The internal motions of integral membrane proteins have largely eluded comprehensive experimental characterization. Here the fast side‐chain dynamics of the α‐helical sensory rhodopsin II and the β‐barrel outer membrane protein W have been investigated in lipid bilayers and detergent micelles by solution NMR relaxation techniques. Despite their differing topologies, both proteins have a similar distribution of methyl‐bearing side‐chain motion that is largely independent of membrane mimetic. The methyl‐bearing side chains of both proteins are, on average, more dynamic in the ps–ns timescale than any soluble protein characterized to date. Accordingly, both proteins retain an extraordinary residual conformational entropy in the folded state, which provides a counterbalance to the absence of the hydrophobic effect. Furthermore, the high conformational entropy could greatly influence the thermodynamics underlying membrane‐protein functions, including ligand binding, allostery, and signaling.

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Sponsoring Organization:: USDOE

Grant/Contract Number:: SC0012704

OSTI ID:: 1632011

Alternate ID(s):: OSTI ID: 1616626

Journal Information:: Angewandte Chemie, Journal Name: Angewandte Chemie Journal Issue: 27 Vol. 132; ISSN 0044-8249

Publisher:: Wiley Blackwell (John Wiley & Sons)Copyright Statement

Country of Publication:: Germany

Language:: English

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