Site-directed13C solid-state NMR studies on membrane proteins: strategy and goals toward revealing conformation and dynamics as illustrated for bacteriorhodopsin labeled with[1-13C]amino acid residues

2004 ◽  
Vol 42 (2) ◽  
pp. 218-230 ◽  
Author(s):  
Hazime Saitô ◽  
Jun Mikami ◽  
Satoru Yamaguchi ◽  
Michikazu Tanio ◽  
Atushi Kira ◽  
...  
Keyword(s):  
Amino Acid ◽  
Solid State ◽  
Membrane Proteins ◽  
Solid State Nmr ◽  
Amino Acid Residues ◽  
Nmr Studies

scholarly journals Gradient reconstitution of membrane proteins for solid-state NMR studies

2017 ◽  
Vol 69 (2) ◽  
pp. 81-91 ◽  
Author(s):  
Denis Lacabanne ◽  
Alons Lends ◽  
Clément Danis ◽  
Britta Kunert ◽  
Marie-Laure Fogeron ◽  
...  
Keyword(s):  
Solid State ◽  
Membrane Proteins ◽  
Solid State Nmr ◽  
Nmr Studies

scholarly journals Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR

Biology ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 396
Author(s):  
Vivien Yeh ◽  
Alice Goode ◽  
Boyan B. Bonev
Keyword(s):  
Protein Structure ◽  
Solid State ◽  
High Resolution ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Solid State Nmr ◽  
Basic Unit ◽  
Molecular Assemblies ◽  
Nmr Studies ◽  
Main Challenge

Biological membranes define the interface of life and its basic unit, the cell. Membrane proteins play key roles in membrane functions, yet their structure and mechanisms remain poorly understood. Breakthroughs in crystallography and electron microscopy have invigorated structural analysis while failing to characterise key functional interactions with lipids, small molecules and membrane modulators, as well as their conformational polymorphism and dynamics. NMR is uniquely suited to resolving atomic environments within complex molecular assemblies and reporting on membrane organisation, protein structure, lipid and polysaccharide composition, conformational variations and molecular interactions. The main challenge in membrane protein studies at the atomic level remains the need for a membrane environment to support their fold. NMR studies in membrane mimetics and membranes of increasing complexity offer close to native environments for structural and molecular studies of membrane proteins. Solution NMR inherits high resolution from small molecule analysis, providing insights from detergent solubilised proteins and small molecular assemblies. Solid-state NMR achieves high resolution in membrane samples through fast sample spinning or sample alignment. Recent developments in dynamic nuclear polarisation NMR allow signal enhancement by orders of magnitude opening new opportunities for expanding the applications of NMR to studies of native membranes and whole cells.

scholarly journals Amino acid type selective isotope labelling of the multidrug ABC transporter LmrA for solid-state NMR studies

FEBS Letters ◽  
2004 ◽  
Vol 568 (1-3) ◽  
pp. 117-121 ◽  
Author(s):  
A James Mason ◽  
Alena Siarheyeva ◽  
Winfried Haase ◽  
Mark Lorch ◽  
Hendrik van Veen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Solid State ◽  
Abc Transporter ◽  
Solid State Nmr ◽  
Amino Acid Type ◽  
Nmr Studies ◽  
Isotope Labelling ◽  
Acid Type
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