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[NMR paper] Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR.
Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR.
Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR.
Chem Commun (Camb). 2013 Feb 26;
Authors: Takaoka Y, Kioi Y, Morito A, Otani J, Arita K, Ashihara E, Ariyoshi M, Tochio H, Shirakawa M, Hamachi I
Abstract
Here we describe how a (19)F-probe incorporated into an endogenous protein by a chemical biology method revealed protein dynamics. By explicit determination of ligand-bound and unbound structures with...
nmrlearner
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02-27-2013 06:47 PM
A 2D 13C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding
A 2D 13C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding
Abstract A 2D 13C Chemical Exchange Saturation Transfer (CEST) experiment is presented for studying slowly exchanging protein systems using methyl groups as probes. The utility of the method is first established through studies of protein L, a small protein, for which chemical exchange on the millisecond time-scale is not observed. Subsequently the approach is applied to a folding exchange reaction of a G48M mutant Fyn SH3 domain, for which only cross-peaks...
nmrlearner
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06-16-2012 06:01 AM
[NMR images] Protein folding technology
http://www.nature.com/horizon/proteinfolding/background/images/technology_f3.jpg
nature.com
29/04/2011 4:32:58 PM GMT
Protein folding technology
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nmrlearner
NMR pictures
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05-22-2011 09:41 PM
[NMR paper] Elucidation of the protein folding landscape by NMR.
Elucidation of the protein folding landscape by NMR.
Related Articles Elucidation of the protein folding landscape by NMR.
Methods Enzymol. 2005;394:299-321
Authors: Dyson HJ, Wright PE
NMR is one of the few experimental methods that can provide detailed insights into the structure and dynamics of unfolded and partly folded states of proteins. Mapping the protein folding landscape is of central importance to understanding the mechanism of protein folding. In addition, it is now recognized that many proteins are intrinsically unstructured in...
nmrlearner
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11-24-2010 11:14 PM
[NMR paper] Contacting the protein folding funnel with NMR.
Contacting the protein folding funnel with NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Contacting the protein folding funnel with NMR.
Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7129-31
Authors: Onuchic JN
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08-22-2010 05:08 PM
[NMR paper] Insights into protein folding from NMR.
Insights into protein folding from NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--arjournals.annualreviews.org-images-AnnualReviews100x25.gif Related Articles Insights into protein folding from NMR.
Annu Rev Phys Chem. 1996;47:369-95
Authors: Dyson HJ, Wright PE
NMR has emerged as an important tool for studies of protein folding because of the unique structural insights it can provide into many aspects of the folding process. Applications include measurements of kinetic folding events and structural characterization of folding...
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08-22-2010 02:27 PM
[NMR paper] An in vitro kinetic assay of ATPase by phosphorus-31 NMR.
An in vitro kinetic assay of ATPase by phosphorus-31 NMR.
Related Articles An in vitro kinetic assay of ATPase by phosphorus-31 NMR.
Kurume Med J. 1990;37(3):153-7
Authors: Chinami M, Shingu M
The ATPase activity of RecA protein was examined by monitoring the changes of NMR phosphorus signals of ATP, ADP and inorganic phosphate. The areas of phosphorus-31 NMR peaks from inorganic phosphate and ADP, which increased with time, and the signals from ATP, which decreased with time, were fitted by a linear least square method to obtain the initial...
nmrlearner
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08-21-2010 10:48 PM
[NMR paper] Prelude to NMR studies of protein folding.
Prelude to NMR studies of protein folding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nsb.gif Related Articles Prelude to NMR studies of protein folding.
Nat Struct Biol. 1999 Jul;6(7):608
Authors: Smith T
in vitro protein folding
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