investigate structure function and dynamics of proteins and nucleic ...
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[NMR paper] Correlation between local structural dynamics of proteins inferred from NMR ensembles and evolutionary dynamics of homologues of known structure.
Correlation between local structural dynamics of proteins inferred from NMR ensembles and evolutionary dynamics of homologues of known structure.
Related Articles Correlation between local structural dynamics of proteins inferred from NMR ensembles and evolutionary dynamics of homologues of known structure.
J Biomol Struct Dyn. 2013 Jun 3;
Authors: Mahajan S, de Brevern AG, Offmann B, Srinivasan N
Abstract
Conformational changes in proteins are extremely important for their biochemical functions. Correlation between inherent conformational...
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06-05-2013 06:53 PM
A Delicate Interplay of Structure, Dynamics, and Thermodynamics for Function: A High Pressure NMR Study of Outer Surface Protein A
A Delicate Interplay of Structure, Dynamics, and Thermodynamics for Function: A High Pressure NMR Study of Outer Surface Protein A
22 February 2012
Publication year: 2012
Source:Biophysical Journal, Volume 102, Issue 4</br>
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Outer surface protein A (OspA) is a crucial protein in the infection of Borrelia burgdorferi causing Lyme disease. We studied conformational fluctuations of OspA with high-pressure 15N/1H two-dimensional NMR along with high-pressure fluorescence spectroscopy. We found evidence within folded, native OspA for rapid local fluctuations of the...
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02-03-2013 10:13 AM
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Proteins. 2011 Oct;79(10):2988-91
Authors: Aramini JM, Rossi P, Fischer M, Xiao R, Acton TB, Montelione GT
Abstract
Protein domain family PF09905 (DUF2132) is a family of small domains of unknown function that are conserved in a wide range of bacteria. Here we describe the solution NMR structure of the 80-residue VF0530 protein from Vibrio fischeri,...
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09-10-2011 06:51 PM
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Molecular simulations and solid-state NMR investigate dynamical structure in rhodopsin activation.
Biochim Biophys Acta. 2011 Aug 8;
Authors: Mertz B, Struts AV, Feller SE, Brown MF
Abstract
Rhodopsin has served as the primary model for studying G protein-coupled receptors (GPCRs)-the largest group in the human genome, and consequently a primary target for pharmaceutical development. Understanding the functions and activation mechanisms of...
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08-20-2011 03:31 PM
Methyl groups as probes of supra-molecular structure, dynamics and function
Methyl groups as probes of supra-molecular structure, dynamics and function
Abstract The development of new protein labeling strategies, along with optimized experiments that exploit the label, have significantly impacted on the types of biochemical problems that can now be addressed by solution NMR spectroscopy. Here we describe how methyl labeling of key residues in a highly deuterated protein background has facilitated studies of the structure, dynamics and interactions of supra-molecular particles. The methyl-labeling approach is briefly reviewed, followed by a summary of...
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01-09-2011 12:46 PM
[NMR paper] Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza
Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.
Related Articles Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.
FEBS Lett. 2003 Nov 27;555(1):139-43
Authors: Tamm LK, Abildgaard F, Arora A, Blad H, Bushweller JH
Recent progress from our laboratories to determine structures of small membrane proteins (up to 20 kDa) in detergent micelles...
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11-24-2010 09:16 PM
[NMR paper] Structure and function of HIV-1 and SIV Tat proteins based on carboxy-terminal trunca
Structure and function of HIV-1 and SIV Tat proteins based on carboxy-terminal truncations, chimeric Tat constructs, and NMR modeling.
Related Articles Structure and function of HIV-1 and SIV Tat proteins based on carboxy-terminal truncations, chimeric Tat constructs, and NMR modeling.
Biomed Pharmacother. 1998;52(10):421-30
Authors: Baier-Bitterlich G, Tretiakova A, Richardson MW, Khalili K, Jameson B, Rappaport J
To further define the structure and function of the domains in HIV-1 and SIV Tat proteins, chimeric Tat cDNA expression constructs...
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11-17-2010 11:06 PM
[NMR paper] Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of
Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of a transcription factor.
Related Articles Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of a transcription factor.
Toxicol Lett. 1995 Dec;82-83:577-89
Authors: Hsu VL, Jia X, Kearns DR
The solution structure of a type II DNA-binding protein (DBPII), transcription factor 1 (TF1), has been determined using NMR spectroscopy. A multidimensional, heteronuclear strategy was employed to overcome assignment ambiguities due to...
investigate structure function and dynamics of proteins and nucleic ...
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