Assignment of the aliphatic proton and carbon-13 resonances of the Bacillus subtilis glucose permease IIA domain using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy

Biochemistry ◽  
1992 ◽  
Vol 31 (18) ◽  
pp. 4413-4425 ◽  
Author(s):  
Wayne J. Fairbrother ◽  
Arthur G. Palmer ◽  
Mark Rance ◽  
Jonathan Reizer ◽  
Milton H. Saier ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Nmr Spectroscopy ◽  
Three Dimensional ◽  
Triple Resonance

Improved resolution in three-dimensional constant-time triple resonance NMR spectroscopy of proteins

1992 ◽  
Vol 2 (1) ◽  
pp. 103-108 ◽  
Author(s):  
Arthur G. Palmer ◽  
Wayne J. Fairbrother ◽  
John Cavanagh ◽  
Peter E. Wright ◽  
Mark Rance
Keyword(s):  
Nmr Spectroscopy ◽  
Three Dimensional ◽  
Constant Time ◽  
Triple Resonance ◽  
Triple Resonance Nmr ◽  
Triple Resonance Nmr Spectroscopy

Assignment of the side-chain proton and carbon-13 resonances of interleukin-1.beta. using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy

Biochemistry ◽  
1990 ◽  
Vol 29 (35) ◽  
pp. 8172-8184 ◽  
Author(s):  
G. Marius Clore ◽  
Ad Bax ◽  
Paul C. Driscoll ◽  
Paul T. Wingfield ◽  
Angela M. Gronenborn
Keyword(s):  
Nmr Spectroscopy ◽  
Interleukin 1 ◽  
Three Dimensional ◽  
Side Chain ◽  
Triple Resonance ◽  
Interleukin 1 Beta

scholarly journals Low resolution solution structure of the Bacillus subtilis glucose permease IIA domain derived from heteronuclear three-dimensional NMR spectroscopy

FEBS Letters ◽  
1992 ◽  
Vol 296 (2) ◽  
pp. 148-152 ◽  
Author(s):  
Wayne J. Fairbrother ◽  
Garry P. Gippert ◽  
Jonathan Reizer ◽  
Milton H. Saier ◽  
Peter E. Wright
Keyword(s):  
Bacillus Subtilis ◽  
Nmr Spectroscopy ◽  
Solution Structure ◽  
Three Dimensional ◽  
Low Resolution

NMR spectroscopy in the conformational analysis of peptides: an overview

2020 ◽  
Vol 27 ◽  
Author(s):  
Marian Vincenzi ◽  
Flavia Anna Mercurio ◽  
Marilisa Leone
Keyword(s):  
Nmr Spectroscopy ◽  
Protein Interactions ◽  
3D Structure ◽  
Theoretical Background ◽  
Triple Resonance ◽  
Protein Protein Interactions ◽  
Nmr Studies ◽  
Conformational Preferences ◽  
Dynamic Perspective ◽  
Nmr Methods

Background: NMR spectroscopy is one of the most powerful tools to study the structure and interaction properties of peptides and proteins from a dynamic perspective. Knowing the bioactive conformations of peptides is crucial in the drug discovery field to design more efficient analogue ligands and inhibitors of protein-protein interactions targeting therapeutically relevant systems. Objective: This review provides a toolkit to investigate peptide conformational properties by NMR. Methods: Articles cited herein, related to NMR studies of peptides and proteins were mainly searched through Pubmed and the web. More recent and old books on NMR spectroscopy written by eminent scientists in the field were consulted as well. Results: The review is mainly focused on NMR tools to gain the 3D structure of small unlabeled peptides. It is more application-oriented as it is beyond its goal to deliver a profound theoretical background. However, the basic principles of 2D homonuclear and heteronuclear experiments are briefly described. Protocols to obtain isotopically labeled peptides and principal triple resonance experiments needed to study them, are discussed as well. Conclusion: NMR is a leading technique in the study of conformational preferences of small flexible peptides whose structure can be often only described by an ensemble of conformations. Although NMR studies of peptides can be easily and fast performed by canonical protocols established a few decades ago, more recently we have assisted to tremendous improvements of NMR spectroscopy to investigate instead large systems and overcome its molecular weight limit.

scholarly journals 2P-022 Investigating protein three-dimensional structures inside living cells by in-cell NMR spectroscopy(The 46th Annual Meeting of the Biophysical Society of Japan)

2008 ◽  
Vol 48 (supplement) ◽  
pp. S78
Author(s):  
Junpei Hamatsu ◽  
Daisuke Sakakibara ◽  
Atsuko Sasaki ◽  
Teppei Ikeya ◽  
Masaki Mishima ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Annual Meeting ◽  
Three Dimensional ◽  
Living Cells ◽  
Biophysical Society

Three-Dimensional Triple-Resonance 1H, 13C, 31P Experiment: Sequential Through-Bond Correlation of Ribose Protons and Intervening Phosphorus along the RNA Oligonucleotide Backbone

1994 ◽  
Vol 116 (14) ◽  
pp. 6472-6473 ◽  
Author(s):  
John P. Marino ◽  
Harald Schwalbe ◽  
Clemens Anklin ◽  
Wolfgang Bermel ◽  
Donald M. Crothers ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Triple Resonance
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