NMR reveals novel mechanisms of protein activity regulation.
NMR reveals novel mechanisms of protein activity regulation.
NMR reveals novel mechanisms of protein activity regulation.
Protein Sci. 2011 Mar 14;
Authors: Kalodimos CG
NMR spectroscopy is one of the most powerful tools for the characterization of biomolecular systems. A unique aspect of NMR is its capacity to provide an integrated insight into both the structure and intrinsic dynamics of biomolecules. In addition, NMR can provide site-resolved information about the conformation entropy of binding, as well as about energetically excited...
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03-16-2011 04:15 PM
[NMR paper] Screening of protein kinases by ATP-STD NMR spectroscopy.
Screening of protein kinases by ATP-STD NMR spectroscopy.
Related Articles Screening of protein kinases by ATP-STD NMR spectroscopy.
J Am Chem Soc. 2005 Jun 8;127(22):7978-9
Authors: McCoy MA, Senior MM, Wyss DF
ATP-STD NMR takes advantage of Mg2+ binding to ATP to adjust the ATP affinity for protein kinases permitting a wide range of Ki's to be determined for ATP competitive ligands. Substituting Mn2+ for Mg2+ creates a paramagnetic probe (MnATP) from which the proximity of non-ATP competitive ligands can be inferred. Internal standards and...
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11-25-2010 08:21 PM
[NMR paper] NMR studies of the sporulation protein SpoIIAA: implications for the regulation of th
NMR studies of the sporulation protein SpoIIAA: implications for the regulation of the transcription factor sigmaF in Bacillus subtilis.
Related Articles NMR studies of the sporulation protein SpoIIAA: implications for the regulation of the transcription factor sigmaF in Bacillus subtilis.
J Biomol NMR. 2001 Apr;19(4):293-304
Authors: Kovacs H, Comfort D, Lord M, Yudkin M, Campbell ID, Nilges M
SpoIIAA participates in a four-component mechanism for phosphorylation-dependent transcription control at the outset of sporulation. We report the...
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11-19-2010 08:32 PM
[NMR paper] Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spec
Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spectral changes observed during phosphorylation of mobile tyrosine residues.
Related Articles Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spectral changes observed during phosphorylation of mobile tyrosine residues.
J Biol Chem. 1991 Jul 15;266(20):13405-10
Authors: Levine BA, Tavaré JM, Alejos E, Clack B, Sayed N
Autophosphorylation of a soluble approximately 48-kDa derivative of the insulin receptor protein-tyrosine kinase...
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[NMR paper] Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spec
Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spectral changes observed during phosphorylation of mobile tyrosine residues.
Related Articles Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spectral changes observed during phosphorylation of mobile tyrosine residues.
J Biol Chem. 1991 Jul 15;266(20):13405-10
Authors: Levine BA, Tavaré JM, Alejos E, Clack B, Sayed N
Autophosphorylation of a soluble approximately 48-kDa derivative of the insulin receptor protein-tyrosine kinase...
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Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York
Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York
A postdoctoral position to study the solution dynamics and structure
of protein kinases is available on a NIH funded project (REF#:
HS-R-6453-10-08-S). Our group is interested in how static and dynamic
changes of protein structure affect the activity of protein kinases.
We combine X-ray crystallography, NMR and ligand binding kinetics with
collaborative molecular dynamic studies (See e.g. ref 1 and 2). Our
research group is located at Stony Brook University in a highly
interactive environment with the New York...
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08-21-2010 05:17 AM
Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York
Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York
A postdoctoral position to study the solution dynamics and structure
of protein kinases is available on a NIH funded project (REF#:
HS-R-6453-10-08-S). Our group is interested in how static and dynamic
changes of protein structure affect the activity of protein kinases.
We combine X-ray crystallography, NMR and ligand binding kinetics with
collaborative molecular dynamic studies (See e.g. ref 1 and 2). Our
research group is located at Stony Brook University in a highly
interactive environment with the New York...
MST1/MST2 Protein Kinases: Regulation and PhysiologicRoles
Linear Mode
