Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues-Reference-Cited by-同舟云学术

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Control of Transmembrane Helix Dynamics by Interfacial Tryptophan Residues

Published:2018-06 Issue:11 Volume:114 Page:2617-2629
ISSN:0006-3495
Container-title:Biophysical Journal
language:en
Short-container-title:Biophysical Journal

Author:

McKay Matthew J.,Martfeld Ashley N.,De Angelis Anna A.,Opella Stanley J.,Greathouse Denise V.,Koeppe Roger E.

Funder

National Institutes of Health

Arkansas Biosciences Institute

Division of Molecular and Cellular Biosciences

Publisher

Elsevier BV

Subject

Biophysics

Reference49 articles.

1. The preference of tryptophan for membrane interfaces;Yau;Biochemistry,1998

2. Engineering the gramicidin channel;Koeppe;Annu. Rev. Biophys. Biomol. Struct,1996

3. Kinetics of gramicidin channel formation in lipid bilayers: transmembrane monomer association;O’Connell;Science,1990

4. The membrane interface dictates different anchor roles for “inner pair” and “outer pair” tryptophan indole rings in gramicidin A channels;Gu;Biochemistry,2011

5. Helix formation and stability in membranes;McKay;Biochim. Biophys. Acta,2018

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