Optimization of amino acid type-specific 13C and 15N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm

2010 ◽  
Vol 49 (2) ◽  
pp. 75-84 ◽  
Author(s):  
Frederik Hefke ◽  
Anurag Bagaria ◽  
Sina Reckel ◽  
Sandra Johanna Ullrich ◽  
Volker Dötsch ◽  
...  
Keyword(s):  
Amino Acid ◽  
Solid State ◽  
Membrane Proteins ◽  
Solid State Nmr ◽  
Backbone Assignment ◽  
Amino Acid Type ◽  
Acid Type ◽  
15N Labeling

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

scholarly journals Structural features of an infectious recombinant PrPSc prion using solid state NMR

2020 ◽  
Author(s):  
Manuel Martín-Pastor ◽  
Yaiza B. Codeseira ◽  
Giovanni Spagnolli ◽  
Hasier Eraña ◽  
Leticia C. Fernández ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Structural Features ◽  
Amino Acid Type ◽  
Atomistic Model ◽  
Secondary Structure Information ◽  
Structure Information ◽  
Nmr Study ◽  
Acid Type ◽  
Deadly Disease

ABSTRACTPrPSc, the first described and most notorious prion, is the only protein known to cause epidemics of deadly disease. Its properties are encoded in its unique structure. Here we report a first solid state NMR study of a uniformly labelled (U-13C,15N)-Bank vole (BV) infectious recombinant PrPSc prion. C-C, C-H and N-H spectra were obtained with MAS rotation of the sample at up to 60 kHz. We obtained amino acid-type secondary structure information and used it to challenge a physically plausible atomistic model of PrPSc consisting of a 4-rung β solenoid recently proposed by us. In all cases, our model was compatible with the data. This study shows that elucidation of the structure of PrPSc is within reach using recombinant PrPSc, NMR, and our model as a guiding tool.

scholarly journals Helix Conformations in 7TM Membrane Proteins Determined Using Oriented-Sample Solid-State NMR with Multiple Residue-Specific 15N Labeling

2008 ◽  
Vol 94 (1) ◽  
pp. 241-250 ◽  
Author(s):  
Thomas Vosegaard ◽  
Miya Kamihira-Ishijima ◽  
Anthony Watts ◽  
Niels Chr. Nielsen
Keyword(s):  
Solid State ◽  
Membrane Proteins ◽  
Solid State Nmr ◽  
Oriented Sample ◽  
15N Labeling

Solid state NMR of membrane proteins: methods and applications

2021 ◽  
Author(s):  
Vivien Yeh ◽  
Boyan B. Bonev
Keyword(s):  
Solid State ◽  
High Resolution ◽  
Membrane Proteins ◽  
Solid State Nmr ◽  
Lipid Membrane ◽  
Cell Function ◽  
Membrane Lipid ◽  
Pharmacological Intervention ◽  
Nmr Methods ◽  
Informative Approach

Membranes of cells are active barriers, in which membrane proteins perform essential remodelling, transport and recognition functions that are vital to cells. Membrane proteins are key regulatory components of cells and represent essential targets for the modulation of cell function and pharmacological intervention. However, novel folds, low molarity and the need for lipid membrane support present serious challenges to the characterisation of their structure and interactions. We describe the use of solid state NMR as a versatile and informative approach for membrane and membrane protein studies, which uniquely provides information on structure, interactions and dynamics of membrane proteins. High resolution approaches are discussed in conjunction with applications of NMR methods to studies of membrane lipid and protein structure and interactions. Signal enhancement in high resolution NMR spectra through DNP is discussed as a tool for whole cell and interaction studies.

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