Cross-Species Analysis of Protein Dynamics Associatedwith Hydride and Proton Transfer in the Catalytic Cycle of the Light-DrivenEnzyme Protochlorophyllide Oxidoreductase
Cross-Species Analysis of Protein Dynamics Associatedwith Hydride and Proton Transfer in the Catalytic Cycle of the Light-DrivenEnzyme Protochlorophyllide Oxidoreductase
LIGHT-SABRE enables efficient in-magnet catalytic hyperpolarization
From The DNP-NMR Blog:
LIGHT-SABRE enables efficient in-magnet catalytic hyperpolarization
Theis, T., et al., LIGHT-SABRE enables efficient in-magnet catalytic hyperpolarization. J Magn Reson, 2014. 248C(0): p. 23-26.
http://www.ncbi.nlm.nih.gov/pubmed/25299767
nmrlearner
News from NMR blogs
0
11-08-2014 12:08 AM
[NMR paper] NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:Quinone oxidoreductase from Vibrio cholerae.
NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:Quinone oxidoreductase from Vibrio cholerae.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_final.gif Related Articles NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:Quinone oxidoreductase from Vibrio cholerae.
J Biol Chem. 2013 Oct 18;288(42):30597-606
Authors: Nedielkov R,...
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis
Abstract The phosphorylation-specific peptidyl-prolyl isomerase Pin1 catalyzes the isomerization of the peptide bond preceding a proline residue between cis and trans isomers. To best understand the mechanisms of Pin1 regulation, rigorous enzymatic assays of isomerization are required. However, most measures of isomerase activity require significant constraints on substrate sequence and only yield rate constants for the cis isomer,
kcatcis and apparent Michaelis constants,
...
nmrlearner
Journal club
0
09-30-2011 08:01 PM
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
J Biomol NMR. 2011 Sep;51(1-2):21-34
Authors: Greenwood AI, Rogals MJ, De S, Lu KP, Kovrigin EL, Nicholson LK
Abstract
The phosphorylation-specific peptidyl-prolyl isomerase Pin1 catalyzes the isomerization of the peptide bond preceding a proline residue between cis and trans isomers. To best understand the mechanisms of Pin1 regulation,...
nmrlearner
Journal club
0
09-30-2011 06:00 AM
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.
J Biomol NMR. 2011 Sep;51(1-2):21-34
Authors: Greenwood AI, Rogals MJ, De S, Lu KP, Kovrigin EL, Nicholson LK
Abstract
The phosphorylation-specific peptidyl-prolyl isomerase Pin1 catalyzes the isomerization of the peptide bond preceding a proline residue between cis and trans isomers. To best understand the mechanisms of Pin1 regulation,...
nmrlearner
Journal club
0
09-30-2011 05:59 AM
[NMR paper] NMR analysis of the interaction between protein L and Ig light chains.
NMR analysis of the interaction between protein L and Ig light chains.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR analysis of the interaction between protein L and Ig light chains.
J Mol Biol. 1997 Jul 4;270(1):8-13
Authors: Enokizono J, Wikström M, Sjöbring U, Björck L, Forsén S, Arata Y, Kato K, Shimada I
Protein L is a cell wall protein expressed by some strains of the anaerobic bacterial species Peptostreptococcus magnus. It binds to immunoglobulin...
nmrlearner
Journal club
0
08-22-2010 05:08 PM
[NMR paper] The importance of binding energy in catalysis of hydride transfer by UDP-galactose 4-
The importance of binding energy in catalysis of hydride transfer by UDP-galactose 4-epimerase: a 13C and 15N NMR and kinetic study.
Related Articles The importance of binding energy in catalysis of hydride transfer by UDP-galactose 4-epimerase: a 13C and 15N NMR and kinetic study.
Biochemistry. 1993 Dec 7;32(48):13220-30
Authors: Burke JR, Frey PA
UDP-galactose 4-epimerase contains NAD+ irreversibly but noncovalently bound to the active site. Uridine nucleotides bind to the substrate site and induce a protein conformational change that...