Related ArticlesMillisecond protein folding studied by NMR spectroscopy.
Protein Pept Lett. 2005 Feb;12(2):139-46
Authors: Zeeb M, Balbach J
Proteins are involved in virtually every biological process and in order to function, it is necessary for these polypeptide chains to fold into the unique, native conformation. This folding process can take place rapidly. NMR line shape analyses and transverse relaxation measurements allow protein folding studies on a microsecond-to-millisecond time scale. Together with an overview of current achievements within this field, we present millisecond protein folding studies by NMR of the cold shock protein CspB from Bacillus subtilis.
Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups.
Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups.
Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups.
J Biomol NMR. 2011 Jun 18;
Authors: Hansen AL, Kay LE
A new pulse sequence is presented for the measurement of relaxation dispersion profiles quantifying millisecond time-scale exchange dynamics of side-chain carbonyl groups in uniformly (13)C labeled proteins. The methodology has...
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[NMR paper] NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements.
NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements.
Related Articles NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements.
J Am Chem Soc. 2005 Sep 28;127(38):13207-12
Authors: Zeeb M, Balbach J
The cold shock protein CspB adopts its native and functional tertiary structure on the millisecond time scale. We employed transverse relaxation NMR methods, which allow a quantitative measurement of the cooperativity of this...
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12-01-2010 06:56 PM
[NMR paper] Unfolded proteins and protein folding studied by NMR.
Unfolded proteins and protein folding studied by NMR.
Related Articles Unfolded proteins and protein folding studied by NMR.
Chem Rev. 2004 Aug;104(8):3607-22
Authors: Dyson HJ, Wright PE
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[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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[NMR paper] Kinetic studies of protein folding using NMR spectroscopy.
Kinetic studies of protein folding using NMR spectroscopy.
Related Articles Kinetic studies of protein folding using NMR spectroscopy.
Nat Struct Biol. 1998 Jul;5 Suppl:504-7
Authors: Dobson CM, Hore PJ
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[NMR paper] Protein complexes studied by NMR spectroscopy.
Protein complexes studied by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein complexes studied by NMR spectroscopy.
Curr Opin Biotechnol. 1996 Aug;7(4):403-8
Authors: Wand AJ, Englander SW
Recent advances in NMR methods now allow protein complexes to be studied in great detail in a wide range of solution conditions. Isotope-enrichment strategies, resonance-assignment approaches and structural-determination methods have evolved to the point...
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[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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[NMR paper] Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR.
Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--arjournals.annualreviews.org-images-AnnualReviews100x25.gif Related Articles Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR.
Annu Rev Biophys Biomol Struct. 1992;21:243-65
Authors: Englander SW, Mayne L
HX-labeling experiments in the pH-pulse mode show that protein folding can be remarkably fast. A near-native form can be reached within milliseconds. Experimental analysis of...
Millisecond protein folding studied by NMR spectroscopy.
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