Publication date: Available online 17 July 2017 Source:Journal of Molecular Biology
Author(s): Yajun Jiang, Charalampos G. Kalodimos
Recent breakthroughs in isotope-labeling and pulse sequence techniques have enabled the Nuclear Magnetic Resonance (NMR) characterization of large protein systems with molecular weights of hundreds of kDa. NMR studies of a great variety of large proteins have provided unique insights into the binding, dynamic, and allosteric mechanisms. Here we present a brief summary of these developments by highlighting few cases that exemplify the uniqueness of NMR in providing atomic-resolution information into key dynamic processes and structures of protein complexes with high degree of flexibility. Graphical abstract
[NMR paper] Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins.
Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins.
Related Articles Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins.
Curr Opin Struct Biol. 2015 Apr 13;32:113-122
Authors: Kerfah R, Plevin MJ, Sounier R, Gans P, Boisbouvier J
Abstract
Nuclear magnetic resonance (NMR) spectroscopy is a uniquely powerful tool for studying the structure, dynamics and interactions of biomolecules at atomic resolution. In the past 15 years, the...
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04-17-2015 08:49 PM
Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins
Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins
Publication date: June 2015
Source:Current Opinion in Structural Biology, Volume 32</br>
Author(s): Rime Kerfah , Michael J Plevin , Remy Sounier , Pierre Gans , Jerome Boisbouvier</br>
Nuclear magnetic resonance (NMR) spectroscopy is a uniquely powerful tool for studying the structure, dynamics and interactions of biomolecules at atomic resolution. In the past 15 years, the development of new isotopic labeling strategies has opened the possibility of exploiting...
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04-14-2015 01:24 PM
[NMR paper] NMR methods for structural studies of large monomeric and multimeric proteins.
NMR methods for structural studies of large monomeric and multimeric proteins.
Related Articles NMR methods for structural studies of large monomeric and multimeric proteins.
Curr Opin Struct Biol. 2013 Jul 11;
Authors: Frueh DP, Goodrich AC, Mishra SH, Nichols SR
Abstract
NMR structural studies of large monomeric and multimeric proteins face distinct challenges. In large monomeric proteins, the common occurrence of frequency degeneracies between residues impedes unambiguous assignment of NMR signals. To overcome this barrier, nonuniform...
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07-16-2013 09:04 PM
NMR methods for structural studies of large monomeric and multimeric proteins
NMR methods for structural studies of large monomeric and multimeric proteins
Publication date: Available online 11 July 2013
Source:Current Opinion in Structural Biology</br>
Author(s): Dominique P Frueh , Andrew C Goodrich , Subrata H Mishra , Scott R Nichols</br>
NMR structural studies of large monomeric and multimeric proteins face distinct challenges. In large monomeric proteins, the common occurrence of frequency degeneracies between residues impedes unambiguous assignment of NMR signals. To overcome this barrier, nonuniform sampling (NUS) is used to...
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07-12-2013 04:06 AM
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies.
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies.
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies.
J Am Chem Soc. 2010 Dec 16;
Authors: Gossert AD, Hiller S, Ferna?ndez C
The detection and structural characterization of protein-ligand interactions by solution NMR is central to functional biology research as well as to drug discovery. Here we present a robust and highly automated procedure for obtaining the resonance assignments necessary for studies of such...
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12-18-2010 12:00 PM
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies
Automated NMR Resonance Assignment of Large Proteins for Protein-Ligand Interaction Studies
Alvar D. Gossert, Sebastian Hiller and Ce?sar Ferna?ndez
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja108383x/aop/images/medium/ja-2010-08383x_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja108383x
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/E3PMYeBSCeE
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[NMR paper] Chain-selective isotopic labeling for NMR studies of large multimeric proteins: appli
Chain-selective isotopic labeling for NMR studies of large multimeric proteins: application to hemoglobin.
Related Articles Chain-selective isotopic labeling for NMR studies of large multimeric proteins: application to hemoglobin.
Biophys J. 2000 Aug;79(2):1146-54
Authors: Simplaceanu V, Lukin JA, Fang TY, Zou M, Ho NT, Ho C
Multidimensional, multinuclear NMR has the potential to elucidate the mechanisms of allostery and cooperativity in multimeric proteins under near-physiological conditions. However, NMR studies of proteins made up of...
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11-19-2010 08:29 PM
[NMR paper] Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N a
Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II.
J Mol Biol. 1996 Dec 20;264(5):1101-16
Authors: Venters RA, Farmer BT, Fierke CA, Spicer LD
Perdeuteration of all non-exchangeable proton sites can...