scholarly journals Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR

2021 ◽  
Author(s):  
Kai Xue ◽  
Kumar Tekwani Movellan ◽  
Xizhou Cecily Zhang ◽  
Eszter E. Najbauer ◽  
Marcel C. Forster ◽  
...  
Keyword(s):  
Solid State ◽  
Membrane Proteins ◽  
Small Molecules ◽  
Lipid Bilayers ◽  
Biological Samples ◽  
Solid State Nmr ◽  
Structure And Function ◽  
Versatile Technique ◽  
And Function

Solid-state NMR (ssNMR) is a versatile technique that can be used for the characterization of various materials, ranging from small molecules to biological samples, including membrane proteins, as reviewed here.

Biophysical methods toolbox to study ABC exporter structure and function

2017 ◽  
Vol 398 (2) ◽  
pp. 229-235
Author(s):  
Thomas Marcellino ◽  
Vasundara Srinivasan
Keyword(s):  
Membrane Proteins ◽  
Abc Transporter ◽  
Integrated Approach ◽  
Structure And Function ◽  
Dynamic Membrane ◽  
Biophysical Characterization ◽  
Intermediate States ◽  
And Function

Abstract ABC exporters are highly dynamic membrane proteins that span a huge spectrum of different conformations. A detailed integrated approach of cellular, biochemical and biophysical characterization of these ‘open’, ‘closed’ and other intermediate states is central to understanding their function. Almost 40 years after the discovery of the first ABC transporter, thanks to the enormous development in methodologies, a picture is slowly emerging to visualize how these fascinating molecules transport their substrates. This mini review summarizes some of the biophysical tools that have made a major impact in understanding the function of the ABC exporters.

scholarly journals Characterization of the Extra-Membrane Domains of CrgA in Lipid Bilayers using Solid State NMR

2019 ◽  
Vol 116 (3) ◽  
pp. 57a
Author(s):  
Yiseul Shin ◽  
Riqiang Fu ◽  
Huajune Qin ◽  
Timothy A. Cross
Keyword(s):  
Solid State ◽  
Lipid Bilayers ◽  
Solid State Nmr ◽  
Membrane Domains

scholarly journals Susceptibility of protein therapeutics to spontaneous chemical modifications by oxidation, cyclization, and elimination reactions

Amino Acids ◽  
2019 ◽  
Vol 51 (10-12) ◽  
pp. 1409-1431 ◽  
Author(s):  
Luigi Grassi ◽  
Chiara Cabrele
Keyword(s):  
Small Molecules ◽  
Three Dimensional ◽  
Drug Market ◽  
Structure And Function ◽  
Dimensional Structure ◽  
Chemical Modifications ◽  
Small Molecule Drugs ◽  
And Function ◽  
The Impact

Abstract Peptides and proteins are preponderantly emerging in the drug market, as shown by the increasing number of biopharmaceutics already approved or under development. Biomolecules like recombinant monoclonal antibodies have high therapeutic efficacy and offer a valuable alternative to small-molecule drugs. However, due to their complex three-dimensional structure and the presence of many functional groups, the occurrence of spontaneous conformational and chemical changes is much higher for peptides and proteins than for small molecules. The characterization of biotherapeutics with modern and sophisticated analytical methods has revealed the presence of contaminants that mainly arise from oxidation- and elimination-prone amino-acid side chains. This review focuses on protein chemical modifications that may take place during storage due to (1) oxidation (methionine, cysteine, histidine, tyrosine, tryptophan, and phenylalanine), (2) intra- and inter-residue cyclization (aspartic and glutamic acid, asparagine, glutamine, N-terminal dipeptidyl motifs), and (3) β-elimination (serine, threonine, cysteine, cystine) reactions. It also includes some examples of the impact of such modifications on protein structure and function.

Methodological development of solid-state NMR for characterization of membrane proteins

2003 ◽  
Vol 18A (2) ◽  
pp. 111-129 ◽  
Author(s):  
M. Bjerring ◽  
T. Vosegaard ◽  
A. Malmendal ◽  
N.C. Nielsen
Keyword(s):  
Solid State ◽  
Membrane Proteins ◽  
Solid State Nmr ◽  
Methodological Development

scholarly journals The power, pitfalls and potential of the nanodisc system for NMR-based studies

2016 ◽  
Vol 397 (12) ◽  
pp. 1335-1354 ◽  
Author(s):  
Aldino Viegas ◽  
Thibault Viennet ◽  
Manuel Etzkorn
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Membrane Proteins ◽  
Lipid Bilayer ◽  
Structure And Function ◽  
Fundamental Importance ◽  
Future Studies ◽  
And Function ◽  
Unique Potential

Abstract The choice of a suitable membrane mimicking environment is of fundamental importance for the characterization of structure and function of membrane proteins. In this respect, usage of the lipid bilayer nanodisc technology provides a unique potential for nuclear magnetic resonance (NMR)-based studies. This review summarizes the recent advances in this field, focusing on (i) the strengths of the system, (ii) the bottlenecks that may be faced, and (iii) promising capabilities that may be explored in future studies.

Solid-State NMR of Membrane Proteins in Lipid Bilayers: To Spin or Not To Spin?

2021 ◽  
Author(s):  
Tata Gopinath ◽  
Daniel Weber ◽  
Songlin Wang ◽  
Erik Larsen ◽  
Gianluigi Veglia
Keyword(s):  
Solid State ◽  
Membrane Proteins ◽  
Lipid Bilayers ◽  
Solid State Nmr
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