[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] Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interact
Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD.
Related Articles Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD.
Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):709-14
Authors: Bann JG, Pinkner J, Hultgren SJ, Frieden C
PapD is a periplasmic chaperone essential for P pilus formation in pyelonephritic strains of E. coli. It is composed of two domains, each of which contains a tryptophan...
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11-24-2010 08:49 PM
[NMR paper] Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.
Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.
Related Articles Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.
FEBS Lett. 1998 Feb 13;423(1):110-2
Authors: Killick TR, Freund SM, Fersht AR
The folding and unfolding of proteins is generally assumed to be so co-operative that the overall process may be followed by a single probe, such as tryptophan fluorescence. Folding kinetics of three mutants of barnase and chymotrypsin inhibitor 2 (CI2) were studied by real-time NMR....
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11-17-2010 11:06 PM
Real-time NMR Studies of the Folding & Mechanisms of Protein Quality Control Machiner
Real-time NMR Studies of the Folding & Mechanisms of Protein Quality Control Machineries
* In the context of a project funded by European Research Council, two postdoctoral positions are available at the Structural Biology Institute in Grenoble (France) to study by real-time NMR the Folding & Mechanisms of Protein Quality Control (PQC) Machineries. Selected candidates will use latest NMR technologies developed at IBS to characterize self-assembly and functionally important structural rearrangements of large PQC machineries isolated at IBS.
* The laboratory host…
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[NMR paper] Real-time refolding studies of 6-19F-tryptophan labeled Escherichia coli dihydrofolat
Real-time refolding studies of 6-19F-tryptophan labeled Escherichia coli dihydrofolate reductase using stopped-flow NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Real-time refolding studies of 6-19F-tryptophan labeled Escherichia coli dihydrofolate reductase using stopped-flow NMR spectroscopy.
Biochemistry. 1996 Dec 24;35(51):16843-51
Authors: Hoeltzli SD, Frieden C
Escherichia coli dihydrofolate reductase (ecDHFR, EC1.5.1.3) contains 5 tryptophan residues that have...
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08-22-2010 02:20 PM
[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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08-22-2010 03:50 AM
[NMR paper] Real-time NMR studies on a transient folding intermediate of barstar.
Real-time NMR studies on a transient folding intermediate of barstar.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Real-time NMR studies on a transient folding intermediate of barstar.
Protein Sci. 1999 Jun;8(6):1286-91
Authors: Killick TR, Freund SM, Fersht AR
The refolding of barstar, the intracellular...