Related ArticlesEvaluation of Solvent Accessibility to the [Fe(4)S(4)] Binding Pocket in Native and Tyr19 Mutant High Potential Iron Proteins by (1)H-(15)N HMQC and (19)F NMR Experiments.
Inorg Chem. 1996 Feb 28;35(5):1121-1125
Authors: Li D, Agarwal A, Cowan JA
The solvent accessibility of Chromatium vinosumhigh potential iron protein (HiPIP) has been investigated by use of (1)H-(15)N HMQC, and (19)F NMR spectroscopy. These NMR experiments indicate that solvent accessibility to the cluster core is similar, and minimal, for the reduced and oxidized states of native HiPIP, but increases significantly for mutant proteins (Tyr19Leu and Tyr19His). These results support a proposed role [Agarwal, A.; Li, D.; Cowan, J. A. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 9440-9444] for Tyr19 in maintaining hydrolytic stability of the [Fe(4)S(4)] cluster, and demonstrate a general strategy for mapping out the solvent accessibility of protein-bound metalloredox prosthetic centers.
PMID: 11666298 [PubMed - as supplied by publisher]
[NMR paper] CORCEMA refinement of the bound ligand conformation within the protein binding pocket
CORCEMA refinement of the bound ligand conformation within the protein binding pocket in reversibly forming weak complexes using STD-NMR intensities.
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J Magn Reson. 2004 May;168(1):36-45
Authors: Jayalakshmi V, Rama Krishna N
We describe an intensity-restrained optimization procedure for refining approximate structures of ligands within the protein binding pockets using STD-NMR...
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[NMR paper] Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy.
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J Biol Chem. 2004 Feb 13;279(7):5699-707
Authors: Olofsson A, Ippel JH, Wijmenga SS, Lundgren E, Ohman A
The human plasma protein transthyretin (TTR) may form fibrillar protein deposits that are associated with both inherited and idiopathic amyloidosis. The present study utilizes solution nuclear magnetic resonance spectroscopy, in combination with...
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[NMR paper] Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy.
Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy.
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Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8648-53
Authors: Ippel JH, Olofsson A, Schleucher J, Lundgren E, Wijmenga SS
Amyloid is the result of an anomalous protein and peptide aggregation, leading to the formation of insoluble fibril deposits. At present, 18 human diseases have been associated with amyloid deposits-e.g., Alzheimer's disease and Prion-transmissible...
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[NMR paper] Refinement of the geometry of the retinal binding pocket in dark-adapted bacteriorhod
Refinement of the geometry of the retinal binding pocket in dark-adapted bacteriorhodopsin by heteronuclear solid-state NMR distance measurements.
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Biochemistry. 2000 Aug 22;39(33):10066-71
Authors: Helmle M, Patzelt H, Ockenfels A, Gärtner W, Oesterhelt D, Bechinger B
The bacterial proton pump bacteriorhodopsin (BR) is a 26.5 kDa seven-transmembrane helical protein. Several...
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[NMR paper] Probing the agonist binding pocket in the nicotinic acetylcholine receptor: a high-re
Probing the agonist binding pocket in the nicotinic acetylcholine receptor: a high-resolution solid-state NMR approach.
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Biochemistry. 1998 Jul 28;37(30):10854-9
Authors: Williamson PT, Gröbner G, Spooner PJ, Miller KW, Watts A
Acetylcholine, the agonist for the nicotinic acetylcholine receptor, has been observed directly when bound specifically to its binding site in the fully functional receptor-enriched...
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Evaluation of protein adsorption and preferred binding regions in multimodal chromato
Evaluation of protein adsorption and preferred binding regions in multimodal chromatography using NMR
Chung, W. K., Freed, A. S., Holstein, M. A., McCallum, S. A., Cramer, S. M....
Date: 2010-09-28
NMR titration experiments with labeled human ubiquitin were employed in concert with chromatographic data obtained with a library of ubiquitin mutants to study the nature of protein adsorption in multimodal (MM) chromatography. The elution order of the mutants on the MM resin was significantly different from that obtained by ion-exchange chromatography. Further, the chromatographic results...
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Crystallographic and NMR evaluation of the impact of peptide binding to the second PD
Crystallographic and NMR evaluation of the impact of peptide binding to the second PDZ domain of PTP1E.
Crystallographic and NMR evaluation of the impact of peptide binding to the second PDZ domain of PTP1E.
Biochemistry. 2010 Sep 14;
Authors: Zhang J, Sapienza PJ, Ke H, Chang A, Hengel SR, Wang H, Phillips GN, Lee AL
PDZ (PSD95/Discs large/ZO-1) domains are ubiquitous protein interaction motifs found in scaffolding proteins involved in signal transduction. Despite the fact that many PDZs show a limited tendency to undergo structural change, the...
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Evaluation of protein adsorption and preferred binding regions in multimodal chromato
Evaluation of protein adsorption and preferred binding regions in multimodal chromatography using NMR.
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Proc Natl Acad Sci U S A. 2010 Sep 13;
Authors: Chung WK, Freed AS, Holstein MA, McCallum SA, Cramer SM
NMR titration experiments with labeled human ubiquitin were employed in concert with chromatographic data obtained with a library of ubiquitin mutants to study the nature of protein adsorption in multimodal (MM) chromatography....
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Evaluation of Solvent Accessibility to the [Fe(4)S(4)] Binding Pocket in Native and T
Linear Mode
