Related ArticlesRecent excitements in protein NMR: Large proteins and biologically relevant dynamics.
J Biosci. 2016 Dec;41(4):787-803
Authors: Chiliveri SC, Deshmukh MV
Abstract
The advent of Transverse Relaxation Optimized SpectroscopY (TROSY) and perdeuteration allowed biomolecular NMR spectroscopists to overcome the size limitation barrier (approx. 20 kDa) in de novo structure determination of proteins. The utility of these techniques was immediately demonstrated on large proteins and protein complexes (e.g. GroELGroES, ClpP protease, Hsp90-p53, 20S proteasome, etc.). Further, recent methodological developments such as Residual Dipolar Couplings and Paramagnetic Relaxation Enhancement allowed accurate measurement of long-range structural restraints. Additionally, Carr-Purcell-Meiboom-Gill (CPMG), rotating frame relaxation experiments (R1(rho)) and saturation transfer experiments (CEST and DEST) created never-before accessibility to the (mu)s-ms timescale dynamic parameters that led to the deeper understanding of biological processes. Meanwhile, the excitement in the field continued with a series of developments in the fast data acquisition methods allowing rapid structural studies on less stable proteins. This review aims to discuss important developments in the field of biomolecular NMR spectroscopy in the recent past, i.e., in the post TROSY era. These developments not only gave access to the structural studies of large protein assemblies, but also revolutionized tools in the arsenal of today's biomolecular NMR and point to a bright future of biomolecular NMR spectroscopy.
[NMR paper] Towards Relatively General and Accurate Quantum Chemical Predictions of Solid-State (17)O NMR Chemical Shifts in Various Biologically Relevant Oxygen-containing Compounds.
Towards Relatively General and Accurate Quantum Chemical Predictions of Solid-State (17)O NMR Chemical Shifts in Various Biologically Relevant Oxygen-containing Compounds.
Towards Relatively General and Accurate Quantum Chemical Predictions of Solid-State (17)O NMR Chemical Shifts in Various Biologically Relevant Oxygen-containing Compounds.
J Phys Chem B. 2015 Aug 14;
Authors: Rorick A, Michael MA, Yang L, Zhang Y
Abstract
Oxygen is an important element in most biologically significant molecules and experimental solid-state...
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Recent advances in magic angle spinning solid state NMR of membrane proteins
From The DNP-NMR Blog:
Recent advances in magic angle spinning solid state NMR of membrane proteins
Wang, S. and V. Ladizhansky, Recent advances in magic angle spinning solid state NMR of membrane proteins. Prog. NMR. Spec., 2014. 82(0): p. 1-26.
http://www.sciencedirect.com/science/article/pii/S0079656514000478
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08-29-2014 05:36 PM
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Top Curr Chem. 2011 Sep 7;
Authors: Ishima R
Abstract
Nuclear Magnetic Resonance (NMR) relaxation is a powerful technique that provides information about internal dynamics associated with configurational energetics in proteins, as well as site-specific information involved in conformational equilibria. In particular, (15)N relaxation is a useful probe to...
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09-08-2011 06:50 PM
Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
Abstract In the last 15 years substantial advances have been made to place isotope labels in native and glycosylated proteins for NMR studies and structure determination. Key developments include segmental isotope labeling using Native Chemical Ligation, Expressed Protein Ligation and Protein Trans-Splicing. These advances are pushing the size limit of NMR spectroscopy further making larger proteins accessible for this technique. It is just emerging that segmental isotope...
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01-09-2011 12:46 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.
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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12-17-2010 12:50 AM
[NMR paper] Determining the structures of large proteins and protein complexes by NMR.
Determining the structures of large proteins and protein complexes by NMR.
Related Articles Determining the structures of large proteins and protein complexes by NMR.
Trends Biotechnol. 1998 Jan;16(1):22-34
Authors: Clore GM, Gronenborn AM
Recent advances in multidimensional NMR methodology to obtain 1H, 15N and 13C resonance assignments, interproton-distance and torsion-angle restraints, and restraints that characterize long-range order have, coupled with new methods of structure refinement, permitted solution structure of proteins in excess...
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11-17-2010 11:06 PM
[NMR paper] NMR structure of a biologically active peptide containing the RNA-binding domain of h
NMR structure of a biologically active peptide containing the RNA-binding domain of human immunodeficiency virus type 1 Tat.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR structure of a biologically active peptide containing the RNA-binding domain of human immunodeficiency virus type 1 Tat.
Proc Natl Acad Sci U S A. 1994 Aug 16;91(17):8248-52
Authors: Mujeeb A, Bishop K, Peterlin BM, Turck C, Parslow TG, James TL
The Tat protein of human...
Recent excitements in protein NMR: Large proteins and biologically relevant dynamics.
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