Related ArticlesProtein stabilization by compatible solutes. Effect of diglycerol phosphate on the dynamics of Desulfovibrio gigas rubredoxin studied by NMR.
Heteronuclear NMR relaxation measurements and hydrogen exchange data have been used to characterize protein dynamics in the presence or absence of stabilizing solutes from hyperthermophiles. Rubredoxin from Desulfovibrio gigas was selected as a model protein and the effect of diglycerol phosphate on its dynamic behaviour was studied. The presence of 100 mM diglycerol phosphate induces a fourfold increase in the half-life for thermal denaturation of D. gigas rubredoxin. A model-free analysis of the protein backbone relaxation parameters shows an average increase of generalized order parameters of 0.015 reflecting a small overall reduction in mobility of fast-scale motions. Hydrogen exchange data acquired over a temperature span of 20 degrees C yielded thermodynamic parameters for the structural opening reactions that allow for the exchange. This shows that the closed form of the protein is stabilized by an additional 1.6 kJ x mol(-1) in the presence of the solute. The results seem to indicate that the stabilizing effect is due mainly to a reduction in mobility of the slower, larger-scale motions within the protein structure with an associated increase in the enthalpy of interactions.
[NMR paper] Chemical proteomic tool for ligand mapping of CYP antitargets: an NMR-compatible 3D Q
Chemical proteomic tool for ligand mapping of CYP antitargets: an NMR-compatible 3D QSAR descriptor in the Heme-Based Coordinate System.
Related Articles Chemical proteomic tool for ligand mapping of CYP antitargets: an NMR-compatible 3D QSAR descriptor in the Heme-Based Coordinate System.
J Chem Inf Comput Sci. 2004 Jul-Aug;44(4):1456-65
Authors: Yao H, Costache AD, Sem DS
Chemical proteomic strategies strive to probe and understand protein-ligand interactions across gene families. One gene family of particular interest in drug and xenobiotic...
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[NMR paper] Prevention of aggregation after refolding by balanced stabilization-destabilization:
Prevention of aggregation after refolding by balanced stabilization-destabilization: production of the Arabidopsis thaliana protein APG8a (At4g21980) for NMR structure determination.
Related Articles Prevention of aggregation after refolding by balanced stabilization-destabilization: production of the Arabidopsis thaliana protein APG8a (At4g21980) for NMR structure determination.
Protein Expr Purif. 2004 Apr;34(2):280-3
Authors: Chae YK, Im H, Zhao Q, Doelling JH, Vierstra RD, Markley JL
The gene coding for APG8a (At4g21980), a protein from...
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[NMR paper] Phosphate ions in bone: identification of a calcium-organic phosphate complex by 31P
Phosphate ions in bone: identification of a calcium-organic phosphate complex by 31P solid-state NMR spectroscopy at early stages of mineralization.
Related Articles Phosphate ions in bone: identification of a calcium-organic phosphate complex by 31P solid-state NMR spectroscopy at early stages of mineralization.
Calcif Tissue Int. 2003 May;72(5):610-26
Authors: Wu Y, Ackerman JL, Strawich ES, Rey C, Kim HM, Glimcher MJ
Previous 31P cross-polarization and differential cross-polarization magic angle spinning (CP/MAS and DCP/MAS) solid-state NMR...
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[NMR paper] NMR evidence for progressive stabilization of native-like structure upon aggregation
NMR evidence for progressive stabilization of native-like structure upon aggregation of acid-denatured LysN.
Related Articles NMR evidence for progressive stabilization of native-like structure upon aggregation of acid-denatured LysN.
J Mol Biol. 2000 Jan 14;295(2):239-55
Authors: Alexandrescu AT, Lamour FP, Jaravine VA
The acid-denatured form of the protein LysN aggregates reversibly at pH 2.0. The strength of self-association increases with increasing Cl(-) anion concentration. At low concentrations of protein or Cl(-) anion, resonances of...
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[NMR paper] Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxi
Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.
Related Articles Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin.
J Biomol NMR. 1994 May;4(3):411-32
Authors: Chandrasekhar K, Campbell AP, Jeng MF, Holmgren A, Dyson HJ
As a prelude to complete structure calculations of both the oxidized and reduced forms of Escherichia coli thioredoxin (M(r) 11,700), we have analyzed the NMR...
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[NMR paper] Transmembrane 19F NMR chemical shift difference of fluorinated solutes in liposomes,
Transmembrane 19F NMR chemical shift difference of fluorinated solutes in liposomes, erythrocytes and erythrocyte ghosts.
Related Articles Transmembrane 19F NMR chemical shift difference of fluorinated solutes in liposomes, erythrocytes and erythrocyte ghosts.
NMR Biomed. 1993 Mar-Apr;6(2):136-43
Authors: Xu AS, Waldeck AR, Kuchel PW
In erythrocytes suspended in isotonic medium, a number of fluorinated anions showed well resolved 19F NMR resonances from the solute populations in the intra- and extracellular compartments; the intracellular...
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[NMR paper] Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using
Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide.
Related Articles Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide.
Biochemistry. 1992 Sep 22;31(37):8790-8
Authors: Sönnichsen FD, Van Eyk JE, Hodges RS, Sykes BD
The structure of a synthetic peptide comprising the 28 amino-terminal residues of actin has been examined by 1H-NMR and CD spectroscopy. The peptide is largely unstructured and flexible in solution but becomes...
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[NMR paper] NMR studies on the 46-kDa dimeric protein, 3,4-dihydroxy-2-butanone 4-phosphate synth
NMR studies on the 46-kDa dimeric protein, 3,4-dihydroxy-2-butanone 4-phosphate synthase, using 2H, 13C, and 15N-labelling.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR studies on the 46-kDa dimeric protein, 3,4-dihydroxy-2-butanone 4-phosphate synthase, using 2H, 13C, and 15N-labelling.
Eur J Biochem. 1999 Apr;261(1):57-65
Authors: Richter G, Kelly M, Krieger C, Yu Y, Bermel W, Karlsson G, Bacher A, Oschkinat H
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Protein stabilization by compatible solutes. Effect of diglycerol phosphate on the dy
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