scholarly journals Increasing the Accuracy of Solution NMR Structures of Membrane Proteins by Application of Residual Dipolar Couplings. High-Resolution Structure of Outer Membrane Protein A

2006 ◽  
Vol 128 (21) ◽  
pp. 6947-6951 ◽  
Author(s):  
Tomasz Cierpicki ◽  
Binyong Liang ◽  
Lukas K. Tamm ◽  
John H. Bushweller
Keyword(s):  
High Resolution ◽  
Membrane Protein ◽  
Residual Dipolar Couplings ◽  
Protein A ◽  
Dipolar Couplings ◽  
Solution Nmr ◽  
Nmr Structures ◽  
High Resolution Structure ◽  
Outer Membrane Protein A ◽  
Resolution Structure

High-Resolution Structure of a Membrane Protein Transferred from Amphipol to a Lipidic Mesophase

2014 ◽  
Vol 247 (9-10) ◽  
pp. 997-1004 ◽  
Author(s):  
V. Polovinkin ◽  
I. Gushchin ◽  
M. Sintsov ◽  
E. Round ◽  
T. Balandin ◽  
...  
Keyword(s):  
High Resolution ◽  
Membrane Protein ◽  
High Resolution Structure ◽  
Resolution Structure

scholarly journals Erratum to: High-Resolution Structure of a Membrane Protein Transferred from Amphipol to a Lipidic Mesophase

2017 ◽  
Vol 250 (2) ◽  
pp. 237-237
Author(s):  
V. Polovinkin ◽  
I. Gushchin ◽  
M. Sintsov ◽  
E. Round ◽  
T. Balandin ◽  
...  
Keyword(s):  
High Resolution ◽  
Membrane Protein ◽  
High Resolution Structure ◽  
Resolution Structure

scholarly journals Detergent-free systems for structural studies of membrane proteins

2021 ◽  
Author(s):  
Youzhong Guo
Keyword(s):  
High Resolution ◽  
Membrane Proteins ◽  
Cell Membrane ◽  
Membrane Protein ◽  
Structural Biology ◽  
Membrane Lipids ◽  
Native Cell ◽  
Lipid Particles ◽  
High Resolution Structure ◽  
Resolution Structure

Membrane proteins play vital roles in living organisms, serving as targets for most currently prescribed drugs. Membrane protein structural biology aims to provide accurate structural information to understand their mechanisms of action. The advance of membrane protein structural biology has primarily relied on detergent-based methods over the past several decades. However, detergent-based approaches have significant drawbacks because detergents often damage the native protein–lipid interactions, which are often crucial for maintaining the natural structure and function of membrane proteins. Detergent-free methods recently have emerged as alternatives with a great promise, e.g. for high-resolution structure determinations of membrane proteins in their native cell membrane lipid environments. This minireview critically examines the current status of detergent-free methods by a comparative analysis of five groups of membrane protein structures determined using detergent-free and detergent-based methods. This analysis reveals that current detergent-free systems, such as the styrene-maleic acid lipid particles (SMALP), the diisobutyl maleic acid lipid particles (DIBMALP), and the cycloalkane-modified amphiphile polymer (CyclAPol) technologies are not better than detergent-based approaches in terms of maintenance of native cell membrane lipids on the transmembrane domain and high-resolution structure determination. However, another detergent-free technology, the native cell membrane nanoparticles (NCMN) system, demonstrated improved maintenance of native cell membrane lipids with the studied membrane proteins, and produced particles that were suitable for high-resolution structural analysis. The ongoing development of new membrane-active polymers and their optimization will facilitate the maturation of these new detergent-free systems.

Overexpression of Outer Membrane Protein A Is a Risk Factor for Mortality in Escherichia coli Bloodstream Infections

2019 ◽  
Author(s):  
Ángel Rodríguez-Villodres ◽  
Rocío Álvarez-Marín ◽  
María Antonia Pérez-Moreno ◽  
Andrea Miró-Canturri ◽  
Marco Durán Lobato ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Risk Factor ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Protein A ◽  
Bloodstream Infections ◽  
Outer Membrane Protein A
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