Related ArticlesDissecting the Microscopic Steps of the Cyclophilin A Enzymatic Cycle on the biological substrate HIV-capsid by NMR.
J Mol Biol. 2010 Aug 11;
Authors: Bosco DA, Eisenmesser EZ, Clarkson MW, Wolf-Watz M, Labeikovsky W, Millet O, Kern D
Peptidyl-prolyl isomerases (PPIases) are emerging as key regulators of many diverse biological processes. Elucidating the role of PPIase activity in vivo has been challenging because mutagenesis of active site residues not only reduces the catalytic activity of these enzymes, but also dramatically affects substrate binding. Employing the cyclophilin A (CypA) PPIase together with its biologically relevant and natively folded substrate, the N-terminal domain of the HIV-1 capsid (CA(N)) protein, we demonstrate here how to dissect residue specific contributions to PPIase catalysis versus substrate binding utilizing NMR spectroscopy. Surprisingly, a number of CypA active-site mutants previously assumed to be strongly diminished in activity toward biological substrates based on a peptide assay only, catalyze the HIV capsid with wild-type activity, but with a change in the rate-limiting step of the enzymatic cycle. The results illustrate that a quantitative analysis of catalysis using the biological substrates is critical when interpreting the effects of PPIase mutations in biological assays.
PMID: 20708627 [PubMed - as supplied by publisher]
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations.
J Biomol NMR. 2011 Sep;51(1-2):5-19
Authors: McIntosh LP, Naito D, Baturin SJ, Okon M, Joshi MD, Nielsen JE
Abstract
NMR-monitored pH titration curves of proteins provide a rich source of structural and electrostatic information. Although relatively straightforward to measure, interpreting pH-dependent chemical shift changes...
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In-cell NMR in E. coli to Monitor Maturation Steps of hSOD1.
In-cell NMR in E. coli to Monitor Maturation Steps of hSOD1.
In-cell NMR in E. coli to Monitor Maturation Steps of hSOD1.
PLoS One. 2011;6(8):e23561
Authors: Banci L, Barbieri L, Bertini I, Cantini F, Luchinat E
Abstract
In-cell NMR allows characterizing the folding state of a protein as well as posttranslational events at molecular level, in the cellular context. Here, the initial maturation steps of human copper, zinc superoxide dismutase 1 are characterized in the E. coli cytoplasm by in-cell NMR: from the apo protein, which is...
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Probing Microscopic Architecture of Opaque Heterogeneous Systems Using Double-Pulsed-Field-Gradient NMR
Probing Microscopic Architecture of Opaque Heterogeneous Systems Using Double-Pulsed-Field-Gradient NMR
Noam Shemesh, Tal Adiri and Yoram Cohen
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja200303h/aop/images/medium/ja-2011-00303h_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja200303h
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/W-dJo6Q8sIM
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[NMR paper] Dissecting functional interactions in coagulation protein complexes by use of NMR spe
Dissecting functional interactions in coagulation protein complexes by use of NMR spectroscopy.
Related Articles Dissecting functional interactions in coagulation protein complexes by use of NMR spectroscopy.
Curr Protein Pept Sci. 2002 Jun;3(3):275-85
Authors: Tolkatchev D, Koutychenko A, Ni F
The blood coagulation cascade can be considered as a system of well-orchestrated protein activation reactions involving and leading to the formation of large macromolecular assemblies. NMR investigations performed during the last six years have focused...
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11-24-2010 08:49 PM
[NMR paper] NMR solution studies of hamster galectin-3 and electron microscopic visualization of
NMR solution studies of hamster galectin-3 and electron microscopic visualization of surface-adsorbed complexes: evidence for interactions between the N- and C-terminal domains.
Related Articles NMR solution studies of hamster galectin-3 and electron microscopic visualization of surface-adsorbed complexes: evidence for interactions between the N- and C-terminal domains.
Biochemistry. 2001 Apr 17;40(15):4859-66
Authors: Birdsall B, Feeney J, Burdett ID, Bawumia S, Barboni EA, Hughes RC
Galectin-3, a beta-galactoside binding protein, contains a...
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11-19-2010 08:32 PM
[NMR paper] Microscopic stability of cold shock protein A examined by NMR native state hydrogen e
Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide.
Related Articles Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide.
Protein Sci. 2000 Feb;9(2):290-301
Authors: Jaravine VA, Rathgeb-Szabo K, Alexandrescu AT
Native state hydrogen exchange of cold shock protein A (CspA) has been characterized as a function of the denaturant urea and of the stabilizing agent...
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11-18-2010 09:15 PM
NMR methods to monitor the enzymatic depolymerization of heparin.
NMR methods to monitor the enzymatic depolymerization of heparin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR methods to monitor the enzymatic depolymerization of heparin.
Anal Bioanal Chem. 2010 Sep 4;
Authors: Limtiaco JF, Beni S, Jones CJ, Langeslay DJ, Larive CK
Heparin and the related glycosaminoglycan, heparan sulfate, are polydisperse linear polysaccharides that mediate numerous biological processes due to their interaction with proteins....
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09-05-2010 05:53 AM
[NMR paper] Efficient enzymatic synthesis of 13C,15N-labeled DNA for NMR studies.
Efficient enzymatic synthesis of 13C,15N-labeled DNA for NMR studies.
Related Articles Efficient enzymatic synthesis of 13C,15N-labeled DNA for NMR studies.
J Biomol NMR. 1997 Oct;10(3):245-53
Authors: Smith DE, Su JY, Jucker FM
The power of heteronuclear NMR spectroscopy to study macromolecules and their complexes has been amply demonstrated over the last decade. The obstacle to routinely applying these techniques to the study of DNA has been the synthesis of 13C,15N-labeled DNA. Here we present a simple and efficient method to generate...
Dissecting the Microscopic Steps of the Cyclophilin A Enzymatic Cycle on the biologic
Linear Mode
