scholarly journals Modeling of the structural features of integral-membrane proteins reverse-environment prediction of integral membrane protein structure (REPIMPS)

2001 ◽  
Vol 10 (8) ◽  
pp. 1529-1538 ◽  
Author(s):  
Siavoush Dastmalchi ◽  
Michael B. Morris ◽  
W. Bret Church
Keyword(s):  
Protein Structure ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Integral Membrane Protein ◽  
Structural Features ◽  
Integral Membrane Proteins ◽  
Membrane Protein Structure

scholarly journals Structures of membrane proteins

2010 ◽  
Vol 43 (1) ◽  
pp. 65-158 ◽  
Author(s):  
Kutti R. Vinothkumar ◽  
Richard Henderson
Keyword(s):  
Protein Structure ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Protein Structures ◽  
Protein Structure Determination ◽  
Membrane Protein Structure ◽  
Expression Systems ◽  
Genome Sequences ◽  
Conformational Variability ◽  
Efficient Expression

AbstractIn reviewing the structures of membrane proteins determined up to the end of 2009, we present in words and pictures the most informative examples from each family. We group the structures together according to their function and architecture to provide an overview of the major principles and variations on the most common themes. The first structures, determined 20 years ago, were those of naturally abundant proteins with limited conformational variability, and each membrane protein structure determined was a major landmark. With the advent of complete genome sequences and efficient expression systems, there has been an explosion in the rate of membrane protein structure determination, with many classes represented. New structures are published every month and more than 150 unique membrane protein structures have been determined. This review analyses the reasons for this success, discusses the challenges that still lie ahead, and presents a concise summary of the key achievements with illustrated examples selected from each class.

Report on the 53rd Annual Meeting of the Canadian Society of Biochemistry, Molecular and Cellular Biology: “Membrane Proteins in Health and Disease”

2011 ◽  
Vol 89 (2) ◽  
pp. 79-81
Author(s):  
Reinhart A.F. Reithmeier ◽  
Joseph R. Casey
Keyword(s):  
Protein Structure ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Protein Trafficking ◽  
Membrane Protein Structure ◽  
Full Spectrum ◽  
Membrane Protein Trafficking ◽  
Bicarbonate Transporters ◽  
Health And Disease ◽  
And Function

The meeting “Membrane Proteins in Health and Disease” featured 6 sessions and 2 satellite meetings. At the opening session, Gunnar von Heijne delivered a plenary lecture entitled Insertion of Membrane Proteins into the Endoplasmic Reticulum. The following session topics were Membrane Protein Trafficking and Folding, Regulation of Membrane Proteins, Membrane Protein Structure, Membrane Proteins in Diverse Species, and Membrane Proteins and Diseases. The satellite meetings discussed bicarbonate transporters and Na+/H+ exchangers. Together the 21 lectures and 106 posters presented at the meeting spanned the full spectrum of current research into membrane protein structure and function.

scholarly journals Selection of Biophysical Methods for Characterisation of Membrane Proteins

2019 ◽  
Vol 20 (10) ◽  
pp. 2605 ◽  
Author(s):  
Tristan O. C. Kwan ◽  
Rosana Reis ◽  
Giuliano Siligardi ◽  
Rohanah Hussain ◽  
Harish Cheruvara ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Early Stage ◽  
Biological Membrane ◽  
Basic Research ◽  
Integral Membrane Protein ◽  
Integral Membrane Proteins ◽  
Functional Protein ◽  
Protein Research ◽  
Selection Of

Over the years, there have been many developments and advances in the field of integral membrane protein research. As important pharmaceutical targets, it is paramount to understand the mechanisms of action that govern their structure–function relationships. However, the study of integral membrane proteins is still incredibly challenging, mostly due to their low expression and instability once extracted from the native biological membrane. Nevertheless, milligrams of pure, stable, and functional protein are always required for biochemical and structural studies. Many modern biophysical tools are available today that provide critical information regarding to the characterisation and behaviour of integral membrane proteins in solution. These biophysical approaches play an important role in both basic research and in early-stage drug discovery processes. In this review, it is not our objective to present a comprehensive list of all existing biophysical methods, but a selection of the most useful and easily applied to basic integral membrane protein research.

scholarly journals Grafted biomembranes containing membrane proteins – the case of the leucine transporter

Soft Matter ◽  
2015 ◽  
Vol 11 (39) ◽  
pp. 7707-7711 ◽  
Author(s):  
Vivien Jagalski ◽  
Robert D. Barker ◽  
Mikkel B. Thygesen ◽  
Kamil Gotfryd ◽  
Mie B. Krüger ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Protein Structure ◽  
Molecular Dynamics Simulation ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Dynamics Simulation ◽  
Membrane Protein Structure ◽  
Neutron Reflection

Together neutron reflection and molecular dynamics simulation offer a powerful tool to study the membrane protein structure in native-like environment.

19F NMR as a versatile tool to study membrane protein structure and dynamics

2019 ◽  
Vol 400 (10) ◽  
pp. 1277-1288 ◽  
Author(s):  
Dania Rose-Sperling ◽  
Mai Anh Tran ◽  
Luca M. Lauth ◽  
Benedikt Goretzki ◽  
Ute A. Hellmich
Keyword(s):  
Protein Structure ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Membrane Protein Structure ◽  
X Ray Crystallography ◽  
Measurement Analysis ◽  
Functional Dynamics ◽  
Ligand Interactions ◽  
Versatile Tool ◽  
G Protein Coupled

AbstractTo elucidate the structures and dynamics of membrane proteins, highly advanced biophysical methods have been developed that often require significant resources, both for sample preparation and experimental analyses. For very complex systems, such as membrane transporters, ion channels or G-protein coupled receptors (GPCRs), the incorporation of a single reporter at a select site can significantly simplify the observables and the measurement/analysis requirements. Here we present examples using19F nuclear magnetic resonance (NMR) spectroscopy as a powerful, yet relatively straightforward tool to study (membrane) protein structure, dynamics and ligand interactions. We summarize methods to incorporate19F labels into proteins and discuss the type of information that can be readily obtained for membrane proteins already from relatively simple NMR spectra with a focus on GPCRs as the membrane protein family most extensively studied by this technique. In the future, these approaches may be of particular interest also for many proteins that undergo complex functional dynamics and/or contain unstructured regions and thus are not amenable to X-ray crystallography or cryo electron microscopy (cryoEM) studies.

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