Related ArticlesResidue-specific real-time NMR diffusion experiments define the association states of proteins during folding.
J Am Chem Soc. 2002 Jun 19;124(24):7156-62
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 association states of unfolded, folded, and intermediate species during protein folding, we have introduced a novel residue-specific real-time NMR diffusion experiment. This experiment, a combination of NMR real-time folding experiments and 3D heteronuclear pulsed field gradient NMR diffusion experiments (LED-HSQC), measures hydrodynamic properties, or molecular sizes, of kinetic species directly during the folding process. Application of the residue-specific real-time NMR diffusion experiments to characterize the folding of the collagen triple helix motif shows that this experiment can be used to determine the association states of unfolded, folded, and kinetic intermediates with transient lifetimes simultaneously. The ratio of the apparent translational diffusion coefficients of the unfolded to the folded form of the triple helix is 0.59, which correlates very well with a theoretical ratio for monomer to linear trimer. The apparent diffusion coefficients of the kinetic intermediates formed during triple helix folding indicate the formation of trimer-like associates which is consistent with previously published kinetic and relaxation data. The residue-specific time dependence of apparent diffusion coefficients of monomer and trimer peaks also illustrates the ability to use diffusion data to probe the directionality of triple helix formation. NMR diffusion experiments provide a new strategy for the investigation of protein-folding mechanisms, both to understand the role of kinetic intermediates and to determine the time-dependent aggregation processes in human diseases.
Real-Time NMR Studies of Electrochemical Double-Layer Capacitors
Real-Time NMR Studies of Electrochemical Double-Layer Capacitors
Hao Wang, Thomas K.-J. Ko?ster, Nicole M. Trease, Julie Se?galini, Pierre-Louis Taberna, Patrice Simon, Yury Gogotsi and Clare P. Grey
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2072115/aop/images/medium/ja-2011-072115_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2072115
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/-UeWTD49pVw
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Transient Enzyme–Substrate Recognition Monitored by Real-Time NMR
Transient Enzyme–Substrate Recognition Monitored by Real-Time NMR
Caroline Haupt, Rica Patzschke, Ulrich Weininger, Stefan Gro?ger, Michael Kovermann and Jochen Balbach
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2010048/aop/images/medium/ja-2011-010048_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2010048
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/nknzYbs0FNE
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06-30-2011 05:01 AM
[NMR paper] Protein folding studied by real-time NMR spectroscopy.
Protein folding studied by real-time NMR spectroscopy.
Related Articles Protein folding studied by real-time NMR spectroscopy.
Methods. 2004 Sep;34(1):65-74
Authors: Zeeb M, Balbach J
Real-time NMR spectroscopy developed to a generally applicable method to follow protein folding reactions. It combines the access to high resolution data with kinetic experiments allowing very detailed insights into the development of the protein structure during different steps of folding. The present review concentrates mainly on the progress of real-time NMR...
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11-24-2010 10:01 PM
[NMR paper] Real-time NMR kinetic studies provide global and residue-specific information on the
Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1beta.
Related Articles Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1beta.
J Mol Biol. 2003 May 2;328(3):693-703
Authors: Roy M, Jennings PA
The interleukin-1beta (IL-1beta) structural motif is a beta-trefoil super fold created by six two-stranded beta-hairpins. Turns are thus...
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11-24-2010 09:01 PM
[NMR paper] NMR exchange broadening arising from specific low affinity protein self-association:
NMR exchange broadening arising from specific low affinity protein self-association: analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1.
Related Articles NMR exchange broadening arising from specific low affinity protein self-association: analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1.
J Biomol NMR. 1999 Aug;14(4):307-20
Authors: Pfuhl M, Chen HA, Kristensen SM, Driscoll PC
Nuclear spin relaxation monitored by heteronuclear NMR provides a useful method to probe the overall and internal molecular motion for...
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11-18-2010 08:31 PM
[NMR paper] Following protein folding in real time using NMR spectroscopy.
Following protein folding in real time using NMR spectroscopy.
Related Articles Following protein folding in real time using NMR spectroscopy.
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...
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08-22-2010 03:50 AM
Assessment of GABARAP self-association by its diffusion properties
Abstract Gamma-aminobutyric acid type A receptor-associated protein (GABARAP) belongs to a family of small ubiquitin-like adaptor proteins implicated in intracellular vesicle trafficking and autophagy. We have used diffusion-ordered nuclear magnetic resonance spectroscopy to study the temperature and concentration dependence of the diffusion properties of GABARAP. Our data suggest the presence of distinct conformational states and provide support for self-association of GABARAP molecules. Assuming a monomerâ??dimer equilibrium, a temperature-dependent dissociation constant could be derived....