[NMR paper] Studying "Invisible" Excited Protein States in Slow Exchange with a Major State Conformation.
From Mendeley Biomolecular NMR group:
Studying "Invisible" Excited Protein States in Slow Exchange with a Major State Conformation.
Journal of the American Chemical Society (2012). Pramodh Vallurupalli, Guillaume Bouvignies, Lewis E Kay et al.
Ever since its initial development, solution NMR spectroscopy has been used as a tool to study conformational exchange. Although many systems are amenable to relaxation dispersion approaches, cases involving highly skewed populations in slow chemical exchange have, in general, remained recalcitrant to study. Here an experiment to detect and...
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08-24-2012 08:01 PM
Structure determination in "shiftless" solid state NMR of oriented protein samples.
Structure determination in "shiftless" solid state NMR of oriented protein samples.
Structure determination in "shiftless" solid state NMR of oriented protein samples.
J Magn Reson. 2011 Jul 6;
Authors: Yin Y, Nevzorov AA
An efficient formalism for calculating protein structures from oriented-sample NMR data in the torsion-angle space is presented. Angular anisotropies of the NMR observables are treated by utilizing an irreducible spherical basis of rotations. An intermediate rotational transformation is introduced that greatly speeds up...
[NMR paper] Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC
Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments.
Related Articles Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments.
J Am Chem Soc. 2002 Oct 16;124(41):12352-60
Authors: Skrynnikov NR, Dahlquist FW, Kay LE
Carr-Purcell-Meiboom-Gill (CPMG) relaxation measurements employing trains of 180 degrees pulses with variable pulse spacing provide valuable information about systems undergoing millisecond-time-scale chemical exchange. Fits of the CPMG relaxation...
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11-24-2010 08:58 PM
[NMR paper] Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein
Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy.
Related Articles Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy.
J Magn Reson. 2000 Oct;146(2):381-4
Authors: Ma C, Opella SJ
Twelve amino acid residues corresponding to an "EF-hand" calcium-binding site were added to the N-terminus of a protein, providing a specific lanthanide ion binding that weakly orients the protein in solution. A...
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11-19-2010 08:29 PM
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...
Protective Protein Is "Guardian Angel" of the Eye - Technology Networks
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