Related ArticlesDynamic NMR spectral analysis and protein folding: identification of a highly populated folding intermediate of rat intestinal fatty acid-binding protein by 19F NMR.
Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):7222-6
Authors: Ropson IJ, Frieden C
The folding of intestinal fatty-acid binding protein has been monitored by 19F NMR after incorporation of 6-fluorotryptophan into the protein. The two resonances resulting from the two tryptophans of this protein showed different dependencies on denaturant concentration. One of the resonances was in slow chemical exchange between two resonance frequencies, native and completely unfolded. The changes for this resonance occurred over a denaturant concentration range identical to that monitored by circular dichroism or fluorescence during unfolding. The other resonance continued to show changes at concentrations of denaturant well above that needed to complete the unfolding transition as monitored by optical techniques. Site directed mutagenesis showed that tryptophan-82 was the residue responsible for the unexpected behavior. We conclude, based on complete line-shape analysis, that there are significant concentrations of one or more intermediates in equilibrium with the native and unfolded forms. The structure of the intermediate(s) is more similar to the completely unfolded form of the protein than to the native structure, since little if any secondary structure is present. Further, these structure(s) persist at high denaturant concentrations and may represent local initiating sites in the folding of this beta-sheet protein.
First solid-state NMR analysis of uniformly (13)C-enriched major light-harvesting complexes from Chlamydomonas reinhardtti and identification of protein and cofactor spin clusters.
First solid-state NMR analysis of uniformly (13)C-enriched major light-harvesting complexes from Chlamydomonas reinhardtti and identification of protein and cofactor spin clusters.
First solid-state NMR analysis of uniformly (13)C-enriched major light-harvesting complexes from Chlamydomonas reinhardtti and identification of protein and cofactor spin clusters.
Biochim Biophys Acta. 2011 Jan 25;
Authors: Pandit A, Morosinotto T, Reus M, Holzwarth AR, Bassi R, de Groot HJ
The light-harvesting complex II (LHCII) is the main component of the...
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NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic.
NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic.
NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic.
Nat Chem Biol. 2011 Jan 23;
Authors: Barb AW, Prestegard JH
The N-glycan at Asn297 of the immunoglobulin G Fc fragment modulates cellular responses of the adaptive immune system. However, the underlying mechanism remains undefined, as existing structural data suggest the glycan does not directly engage cell surface receptors. Here we characterize the dynamics of the glycan termini...
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[NMR paper] The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 vis
The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 visualized by NMR and docking using HADDOCK.
Related Articles The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 visualized by NMR and docking using HADDOCK.
Protein Sci. 2005 Mar;14(3):799-811
Authors: Volkov AN, Ferrari D, Worrall JA, Bonvin AM, Ubbink M
The interaction of bovine microsomal ferricytochrome b5 with yeast iso-1-ferri and ferrocytochrome c has been investigated using heteronuclear NMR techniques. Chemical-shift...
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[NMR paper] Inverse methods in two-dimensional NMR spectral analysis.
Inverse methods in two-dimensional NMR spectral analysis.
Related Articles Inverse methods in two-dimensional NMR spectral analysis.
J Magn Reson. 2003 May;162(1):141-57
Authors: van Beek JD, Meier BH, Schäfer H
Solid-state NMR is a valuable technique for the study of disordered materials. Analysis of such spectra usually involves solution of so-called ill-posed inverse problems. Here we present a strategy for the analysis of two-parameter two-dimensional NMR problems and test it on 2D DECODER and DOQSY experiments. Using Monte Carlo tests,...
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[NMR paper] Initiation sites of protein folding by NMR analysis.
Initiation sites of protein folding by NMR analysis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Initiation sites of protein folding by NMR analysis.
Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10600-3
Authors: Freund SM, Wong KB, Fersht AR
Detailed characterization of denatured states of proteins is necessary to understand the interactions that funnel the large number of possible conformations along fast routes for folding. Nuclear magnetic resonance...
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[NMR paper] Dynamic NMR studies of ligand-receptor interactions: design and analysis of a rapidly
Dynamic NMR studies of ligand-receptor interactions: design and analysis of a rapidly exchanging complex of FKBP-12/FK506 with a 24 kDa calcineurin fragment.
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 Dynamic NMR studies of ligand-receptor interactions: design and analysis of a rapidly exchanging complex of FKBP-12/FK506 with a 24 kDa calcineurin...
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[NMR paper] 1H NMR identification of a beta-sheet structure and description of folding topology i
1H NMR identification of a beta-sheet structure and description of folding topology in putidaredoxin.
Related Articles 1H NMR identification of a beta-sheet structure and description of folding topology in putidaredoxin.
Biochemistry. 1991 Apr 23;30(16):3850-6
Authors: Pochapsky TC, Ye XM
Putidaredoxin (Pdx), a 106-residue globular protein consisting of a single polypeptide chain and a cluster, is the physiological reductant of P-450cam, which in turn catalyzes the monohydroxylation of camphor by molecular oxygen. No crystal structure has...
Dynamic NMR spectral analysis and protein folding: identification of a highly populat
Linear Mode
