Literature DB >> 9257681

The conformational preference of gramicidin channels is a function of lipid bilayer thickness.

N Mobashery1, C Nielsen, O S Andersen.   

Abstract

In order to understand how the material properties of lipid bilayers could affect integral membrane protein function, we examined the effect of a hydrophobic mismatch on the structure and function of membrane-spanning gramicidin channels. Changes in lipid bilayer thickness affect the conformational preference of membrane-spanning gramicidin A (gA) channels (single-stranded [SS] dimers <--> double-stranded [DS] dimers) and induces an additional conductance state in the standard (SS) beta6.3-helical channel. These results provide experimental evidence for the importance of energetic coupling between the bilayer and imbedded inclusions.

Entities:  

Mesh：

Substances：

Year:  1997        PMID： 9257681     DOI： 10.1016/s0014-5793(97)00709-6

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  35 in total

1.  Desformylgramicidin: a model channel with an extremely high water permeability.

Authors:  S M Saparov; Y N Antonenko; R E Koeppe; P Pohl
Journal:  Biophys J       Date:  2000-11       Impact factor: 4.033

2.  Gramicidin A channels switch between stretch activation and stretch inactivation depending on bilayer thickness.

Authors:  Boris Martinac; Owen P Hamill
Journal:  Proc Natl Acad Sci U S A       Date:  2002-03-19       Impact factor: 11.205

3.  Bilayer thickness modulates the conductance of the BK channel in model membranes.

Authors:  Chunbo Yuan; Robert J O'Connell; Paula L Feinberg-Zadek; Linda J Johnston; Steven N Treistman
Journal:  Biophys J       Date:  2004-06       Impact factor: 4.033

4.  The pH-dependent induction of lipid membrane ionic permeability by N-terminally lysine-substituted analogs of gramicidin A.

Authors:  Tatyana I Rokitskaya; Alexandra I Sorochkina; Sergey I Kovalchuk; Natalya S Egorova; Elena A Kotova; Sergey V Sychev; Yuri N Antonenko
Journal:  Eur Biophys J       Date:  2011-11-01       Impact factor: 1.733

5.  The antimicrobial peptide gramicidin S permeabilizes phospholipid bilayer membranes without forming discrete ion channels.

Authors:  Md Ashrafuzzaman; O S Andersen; R N McElhaney
Journal:  Biochim Biophys Acta       Date:  2008-09-05

Review 6.  Swimming through the hydrophobic sea: new insights in protein translocation.

Authors:  J A Mindell
Journal:  Proc Natl Acad Sci U S A       Date:  1998-04-14       Impact factor: 11.205

7.  The Water Permeability and Pore Entrance Structure of Aquaporin-4 Depend on Lipid Bilayer Thickness.

Authors:  Jihong Tong; Zhe Wu; Margaret M Briggs; Klaus Schulten; Thomas J McIntosh
Journal:  Biophys J       Date:  2016-07-12       Impact factor: 4.033

8.  Spin-labeled gramicidin a: channel formation and dissociation.

Authors:  Boris G Dzikovski; Petr P Borbat; Jack H Freed
Journal:  Biophys J       Date:  2004-08-23       Impact factor: 4.033

9.  Structural restraints and heterogeneous orientation of the gramicidin A channel closed state in lipid bilayers.

Authors:  Y Mo; T A Cross; W Nerdal
Journal:  Biophys J       Date:  2004-05       Impact factor: 4.033

Review 10.  Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes.

Authors:  Jens A Lundbaek; Shemille A Collingwood; Helgi I Ingólfsson; Ruchi Kapoor; Olaf S Andersen
Journal:  J R Soc Interface       Date:  2009-11-25       Impact factor: 4.118
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.