Fast Real-Time NMR Methods for Characterizing Short-Lived Molecular States.
Chemphyschem. 2013 Jul 15;
Authors: Rennella E, Brutscher B
Abstract
The characterization of both the structure and the conformational dynamics of biological macromolecules, namely proteins and nucleic acids, is required for understanding the molecular mechanisms underlying physiological function and disease. Molecular dynamics involves the transient departure from the ground-state structures to populate short-lived excited state conformations that can play important functional roles. Real-time multi-dimensional NMR spectroscopy represents a unique tool for investigating dynamic molecular processes occurring on time scales of seconds or longer, providing atomic-resolution information about short-lived states. In this minireview, we discuss recent progress made in the field of fast real-time multidimensional NMR. The potential of these new methods is illustrated for several biomolecular systems that have recently been studied by fast real-time multidimensional NMR.
PMID: 23857553 [PubMed - as supplied by publisher]
Boosting the Sensitivityof Ligand–ProteinScreening by NMR of Long-Lived States
Boosting the Sensitivityof Ligand–ProteinScreening by NMR of Long-Lived States
Nicola Salvi, Roberto Buratto, Aure?lien Bornet, Simone Ulzega, Inmaculada Rentero Rebollo, Alessandro Angelini, Christian Heinis and Geoffrey Bodenhausen
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja303301w/aop/images/medium/ja-2012-03301w_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja303301w
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/xsuzyMhXJF4
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Long-Lived States to Monitor Protein Unfolding by Proton NMR.
Long-Lived States to Monitor Protein Unfolding by Proton NMR.
Long-Lived States to Monitor Protein Unfolding by Proton NMR.
Chemphyschem. 2011 Aug 31;
Authors: Bornet A, Ahuja P, Sarkar R, Fernandes L, Hadji S, Lee SY, Haririnia A, Fushman D, Bodenhausen G, Vasos PR
Abstract
The relaxation of long-lived states (LLS) corresponds to the slow return to statistical thermal equilibrium between symmetric and antisymmetric proton spin states. This process is remarkably sensitive to the presence of external spins and can be used to obtain...
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09-02-2011 05:40 PM
[NMR paper] Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic eve
Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds.
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J Am Chem Soc. 2005 Jun 8;127(22):8014-5
Authors: Schanda P, Brutscher B
We demonstrate for different protein samples that 2D 1H-15N correlation NMR spectra can be recorded in a few seconds of acquisition time using a new band-selective optimized flip-angle...
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[NMR paper] A high-resolution NMR study of long-lived water molecules in both oxidation states of
A high-resolution NMR study of long-lived water molecules in both oxidation states of a minimal cytochrome c.
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Biochemistry. 2003 Apr 1;42(12):3457-63
Authors: Bertini I, Ghosh K, Rosato A, Vasos PR
The interaction of water with oxidized and reduced cytochrome c from the Gram-positive bacterium Bacillus pasteurii (a 71-amino acid long monoheme cytochrome) is investigated through CLEANEX experiments and (15)N-edited...
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Authors: Buevich AV, Baum J
Characterizing the association states of proteins during folding is critical for understanding the nature of protein-folding intermediates and protein-folding pathways, protein aggregation, and disease-related aggregation. To study the...
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11-24-2010 08:49 PM
Scientist develops new, innovative methods for characterizing proteins - Eureka! Scie
Scientist develops new, innovative methods for characterizing proteins - Eureka! Science News
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Eureka! Science News
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Scientist develops new, innovative methods for characterizing proteins
Eureka! Science News
Nuclear magnetic resonance (NMR) data are first collected for a particular protein that is being analyzed. (NMR is a research tool that utilizes high ...
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Nat Struct Biol. 1995 Oct;2(10):865-70
Authors: Balbach J, Forge V, van Nuland NA, Winder SL, Hore PJ, Dobson CM
The refolding of apo bovine alpha-lactalbumin has been monitored in real time by NMR spectroscopy following rapid in situ dilution of a chemically denatured state. By examining individual resonances in the time-resolved NMR spectra, the native state has been shown to emerge in a cooperative...
Fast Real-Time NMR Methods for Characterizing Short-Lived Molecular States.
Linear Mode
