scholarly journals Efficiency of detergents at maintaining membrane protein structures in their biologically relevant forms

2012 ◽  
Vol 1818 (5) ◽  
pp. 1351-1358 ◽  
Author(s):  
David V. Tulumello ◽  
Charles M. Deber
Keyword(s):  
Membrane Protein ◽  
Protein Structures ◽  
Biologically Relevant

Simulation studies of the interactions between membrane proteins and detergents

2005 ◽  
Vol 33 (5) ◽  
pp. 910-912 ◽  
Author(s):  
P.J. Bond ◽  
J. Cuthbertson ◽  
M.S.P. Sansom
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Self Assembly ◽  
Kinetic Mechanism ◽  
Coarse Grained ◽  
Simulation Studies ◽  
High Resolution Data ◽  
Biologically Relevant ◽  
Structure And Dynamics ◽  
Detergent Interactions

Interactions between membrane proteins and detergents are important in biophysical and structural studies and are also biologically relevant in the context of folding and transport. Despite a paucity of high-resolution data on protein–detergent interactions, novel methods and increased computational power enable simulations to provide a means of understanding such interactions in detail. Simulations have been used to compare the effect of lipid or detergent on the structure and dynamics of membrane proteins. Moreover, some of the longest and most complex simulations to date have been used to observe the spontaneous formation of membrane protein–detergent micelles. Common mechanistic steps in the micelle self-assembly process were identified for both α-helical and β-barrel membrane proteins, and a simple kinetic mechanism was proposed. Recently, simplified (i.e. coarse-grained) models have been utilized to follow long timescale transitions in membrane protein–detergent assemblies.

scholarly journals Phasing statistics for alpha helical membrane protein structures

2013 ◽  
Vol 22 (11) ◽  
pp. 1664-1668 ◽  
Author(s):  
Joanne L. Parker ◽  
Simon Newstead
Keyword(s):  
Membrane Protein ◽  
Protein Structures

Mutations in transmembrane proteins: diseases, evolutionary insights, prediction and comparison with globular proteins

2020 ◽  
Author(s):  
Jan Zaucha ◽  
Michael Heinzinger ◽  
A Kulandaisamy ◽  
Evans Kataka ◽  
Óscar Llorian Salvádor ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Lipid Bilayers ◽  
Protein Structures ◽  
Experimental Studies ◽  
Single Amino Acid ◽  
Evolutionary Information ◽  
Missense Variants ◽  
Current State ◽  
Aqueous Environments

Abstract Membrane proteins are unique in that they interact with lipid bilayers, making them indispensable for transporting molecules and relaying signals between and across cells. Due to the significance of the protein’s functions, mutations often have profound effects on the fitness of the host. This is apparent both from experimental studies, which implicated numerous missense variants in diseases, as well as from evolutionary signals that allow elucidating the physicochemical constraints that intermembrane and aqueous environments bring. In this review, we report on the current state of knowledge acquired on missense variants (referred to as to single amino acid variants) affecting membrane proteins as well as the insights that can be extrapolated from data already available. This includes an overview of the annotations for membrane protein variants that have been collated within databases dedicated to the topic, bioinformatics approaches that leverage evolutionary information in order to shed light on previously uncharacterized membrane protein structures or interaction interfaces, tools for predicting the effects of mutations tailored specifically towards the characteristics of membrane proteins as well as two clinically relevant case studies explaining the implications of mutated membrane proteins in cancer and cardiomyopathy.

scholarly journals Design Principles of Membrane Protein Structures

2016 ◽  
Vol 110 (3) ◽  
pp. 56a
Author(s):  
Diane Nguyen ◽  
Vladimir Yarov-Yarovoy
Keyword(s):  
Membrane Protein ◽  
Protein Structures ◽  
Design Principles

Recent Advances in Membrane Biochemistry

2011 ◽  
Vol 39 (3) ◽  
pp. 703-706 ◽  
Author(s):  
J. Malcolm East ◽  
Francesco Michelangeli
Keyword(s):  
Membrane Protein ◽  
Structure Function ◽  
Human Health ◽  
Membrane Structure ◽  
Protein Structures ◽  
Annual Symposium ◽  
Recent Advances ◽  
Society Annual

This Biochemical Society Annual Symposium on Recent Advances in Membrane Biochemistry was organized to bring together experts from across the spectrum of biomembrane disciplines from the biological to the biophysical/structural, with the intention of promoting interactions and collaborations across the field. We were keen that the potential for improving human health that stems from a deeper understanding of membrane structure/function should be acknowledged, especially in the light of the increasing numbers of membrane protein structures that continue to be made available to the biomembrane community. This foreword provides an idea of what was communicated in the various sessions and, we hope, gives an impression of the excitement generated by the speakers and delegates at this over-subscribed Symposium.

scholarly journals MemProtMD: Membrane Protein Structures and Simulations

2014 ◽  
Vol 106 (2) ◽  
pp. 634a ◽  
Author(s):  
Phillip J. Stansfeld ◽  
Mark S.P. Sansom
Keyword(s):  
Membrane Protein ◽  
Protein Structures

Membrane Protein Structures 2015 Meeting

2016 ◽  
Vol 29 (1) ◽  
pp. 19-20
Author(s):  
Robert F. Fischetti
Keyword(s):  
Membrane Protein ◽  
Protein Structures

scholarly journals Influence of solubilizing environments on membrane protein structures

2011 ◽  
Vol 36 (2) ◽  
pp. 117-125 ◽  
Author(s):  
Timothy A. Cross ◽  
Mukesh Sharma ◽  
Myunggi Yi ◽  
Huan-Xiang Zhou
Keyword(s):  
Membrane Protein ◽  
Protein Structures
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