Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy

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.

Location
Deutsche Nationalbibliothek Frankfurt am Main
Extent
Online-Ressource
Language
Englisch

Bibliographic citation
Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy ; volume:132 ; number:27 ; year:2020 ; pages:11201-11207 ; extent:7
Angewandte Chemie ; 132, Heft 27 (2020), 11201-11207 (gesamt 7)

Creator
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
URN
urn:nbn:de:101:1-2022052911314389304679
Rights
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Last update
15.08.2025, 7:29 AM CEST

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Associated

  • 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

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