Real-time NMR monitoring of protein-folding kinetics by a recycle flow system for temperature jump.
Anal Chem. 2013 Sep 12;
Authors: Yamasaki K, Obara Y, Hasegawa M, Tanaka H, Yamasaki T, Wakuda T, Okada M, Kohzuma T
Abstract
An NMR method was developed that allows for real-time monitoring of reactions (on the order of seconds) induced by temperature jump. In a recycle flow system, heating and cooling baths were integrated, with the latter inside the NMR probe. A refolding reaction of ribonuclease A was triggered by rapid cooling and monitored by a series of NMR measurements over 12 s. Data were processed by principal component analysis, in which a factor related to the structural change with an exponential rate constant of 0.2-0.7 s-1 was successfully separated from factors related to baseline instability and/or noise. Temperature dependency of the rate constant revealed the entropy-driven formation of the transition state of the refolding reaction.
PMID: 24028433 [PubMed - as supplied by publisher]
[NMR paper] Effect of Internal Cavities on Folding Rates and Routes Revealed by Real-time Pressure-Jump NMR Spectroscopy.
Effect of Internal Cavities on Folding Rates and Routes Revealed by Real-time Pressure-Jump NMR Spectroscopy.
Effect of Internal Cavities on Folding Rates and Routes Revealed by Real-time Pressure-Jump NMR Spectroscopy.
J Am Chem Soc. 2013 Aug 30;
Authors: Roche J, Dellarole M, Caro JA, Norberto DR, Garcia AE, Garcia-Moreno E B, Roumestand C, Royer CA
Abstract
The time required to fold proteins usually increases significantly under conditions of high pressure. Taking advantage of this general property of proteins, we combined P-jump...
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[NMR paper] Real-time kinetics of high-mobility group box 1 oxidation in extracellular fluids studied by in situ protein NMR spectroscopy.
Real-time kinetics of high-mobility group box 1 oxidation in extracellular fluids studied by in situ protein NMR spectroscopy.
Real-time kinetics of high-mobility group box 1 oxidation in extracellular fluids studied by in situ protein NMR spectroscopy.
J Biol Chem. 2013 Feb 27;
Authors: Zandarashvili L, Sahu D, Lee K, Lee YS, Singh P, Rajarathnam K, Iwahara J
Abstract
Some extracellular proteins are initially secreted in the reduced form via a non-canonical pathway bypassing the endoplasmic reticulum, and become oxidized in the...
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[NMR paper] Protein folding studied by real-time NMR spectroscopy.
Protein folding studied by real-time NMR spectroscopy.
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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] Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
Related Articles Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
J Mol Biol. 2003 May 16;328(5):1161-71
Authors: Mizuguchi M, Kroon GJ, Wright PE, Dyson HJ
At low ionic strength, apoplastocyanin forms an unfolded state under non-denaturing conditions. The refolding of this state is sufficiently slow to allow real-time NMR experiments to be performed. Folding of apoplastocyanin, initiated by the addition of salt and followed by real-time 2D 1H-15N...
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11-24-2010 09:01 PM
[NMR paper] Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optic
Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy.
Related Articles Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy.
J Mol Biol. 1998 Feb 27;276(3):657-67
Authors: Guijarro JI, Morton CJ, Plaxco KW, Campbell ID, Dobson CM
The refolding kinetics of the chemically denatured SH3 domain of phosphatidylinositol 3'-kinase (PI3-SH3) have been monitored by real-time one-dimensional 1H NMR coupled with a variety of other biophysical techniques. These...
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11-17-2010 11:06 PM
[NMR paper] Following protein folding in real time using NMR spectroscopy.
Following protein folding in real time using NMR spectroscopy.
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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...
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08-22-2010 03:50 AM
[NMR paper] Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labele
Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase.
Proc Natl Acad Sci U S A. 1995 Sep 26;92(20):9318-22
Authors: Hoeltzli SD, Frieden C
Escherichia coli dihydrofolate reductase (DHFR; EC 1.5.1.3) contains...
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[NMR paper] Temperature-jump NMR study of protein folding: ribonuclease A at low pH.
Temperature-jump NMR study of protein folding: ribonuclease A at low pH.
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J Biomol NMR. 1991 May;1(1):65-70
Authors: Akasaka K, Naito A, Nakatani H
The kinetic process of folding of bovine pancreatic ribonuclease A in a 2H2O environment at pH 1.2 was examined by a recently developed temperature-jump NMR method (Akasaka et al., (1990) Rev. Sci. Instrum. 61, 66-68). Upon temperature-jump down from 45 degrees C to 29 degrees C, which was attained within 6 s,...
Real-time NMR monitoring of protein-folding kinetics by a recycle flow system for temperature jump.
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