[NMR paper] NMR Characterization of the Interaction of the Endonuclease Domain of MutL with Divalent Metal Ions and ATP.
NMR Characterization of the Interaction of the Endonuclease Domain of MutL with Divalent Metal Ions and ATP.
Related Articles NMR Characterization of the Interaction of the Endonuclease Domain of MutL with Divalent Metal Ions and ATP.
PLoS One. 2014;9(6):e98554
Authors: Mizushima R, Kim JY, Suetake I, Tanaka H, Takai T, Kamiya N, Takano Y, Mishima Y, Tajima S, Goto Y, Fukui K, Lee YH
Abstract
MutL is a multi-domain protein comprising an N-terminal ATPase domain (NTD) and C-terminal dimerization domain (CTD), connected with...
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06-06-2014 03:59 PM
[NMR paper] Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.
Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.
Related Articles Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.
J Biomol NMR. 2013 Apr 23;
Authors: Chakravorty DK, Wang B, Lee CW, Guerra AJ, Giedroc DP, Merz KM
Abstract
Correctly calculating the structure of metal coordination sites in a protein during the process of nuclear magnetic resonance (NMR) structure determination and refinement continues to...
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04-24-2013 09:48 PM
Interactions of gemini surfactants with two model proteins: NMR, CD, and fluorescence spectroscopies
Interactions of gemini surfactants with two model proteins: NMR, CD, and fluorescence spectroscopies
1 March 2012
Publication year: 2012
Source:Journal of Colloid and Interface Science, Volume 369, Issue 1</br>
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Gemini surfactants have two polar head groups and two hydrocarbon tails. Compared with conventional surfactants, geminis have much lower (?M vs. mM) critical micelle concentrations and possess slower (ms vs. ?s) monomer ? micelle kinetics. The structure of the gemini surfactants studied is ·2Br- where s =4, 5, or 6. Our objective is to reveal the effect...
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02-03-2013 10:13 AM
Characterization of the ground state dynamics of proteorhodopsin by NMR and optical spectroscopies
Characterization of the ground state dynamics of proteorhodopsin by NMR and optical spectroscopies
Abstract We characterized the dynamics of proteorhodopsin (PR), solubilized in diC7PC, a detergent micelle, by liquid-state NMR spectroscopy at T = 323 K. Insights into the dynamics of PR at different time scales could be obtained and dynamic hot spots could be identified at distinct, functionally relevant regions of the protein, including the BC loop, the EF loop, the N-terminal part of helix F and the C-terminal part of helix G. We further characterize the dependence of the photocycle...
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11-22-2012 05:27 AM
NMR Spectroscopies Loc: North West with Science and Technology ...
NMR Spectroscopies Loc: North West with Science and Technology ...
Employer: Science and Technology Recruitment, Location: North West region, ID: 1401333740, Hours: Full Time, Contract type: Permanent, Date posted: 31 Jan ...
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02-06-2012 03:54 PM
[NMR paper] Metal binding sites in proteins: identification and characterization by paramagnetic NMR relaxation.
Metal binding sites in proteins: identification and characterization by paramagnetic NMR relaxation.
Related Articles Metal binding sites in proteins: identification and characterization by paramagnetic NMR relaxation.
Biochemistry. 2005 Aug 23;44(33):11014-23
Authors: Jensen MR, Petersen G, Lauritzen C, Pedersen J, Led JJ
A method is presented that allows the identification and quantitative characterization of metal binding sites in proteins using paramagnetic nuclear magnetic resonance spectroscopy. The method relies on the nonselective...
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12-01-2010 06:56 PM
[NMR paper] Conformational variation of the central CG site in d(ATGACGTCAT)2 and d(GAAAACGTTTTC)
Conformational variation of the central CG site in d(ATGACGTCAT)2 and d(GAAAACGTTTTC)2. An NMR, molecular modelling and 3D-homology investigation.
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 Conformational variation of the central CG site in d(ATGACGTCAT)2 and d(GAAAACGTTTTC)2. An NMR, molecular modelling and 3D-homology investigation.
Eur J Biochem. 1999 May;261(3):722-33
Authors: Cordier C, Marcourt L, Petitjean M, Dodin G
...
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08-21-2010 04:03 PM
CSA variation: how reliable model-free dynamics is
The following paper shows, in particular, how site-specific variations of 15N chemical shift anisotropy (CSA) can cause under- and overestimation of protein mobility that is inferred from the order parameter of model-free analysis.
Limited variations in 15N CSA magnitudes and orientations in ubiquitin are revealed by joint analysis of longitudinal and transverse NMR relaxation.
Damberg P, Jarvet J, Graslund A.
Department of Biochemistry and Biophysics, Stockholm University, Svante Arrheniusv.12, S-106 91 Stockholm, Sweden.
J Am Chem Soc. 2005 Feb 16;127(6):1995-2005.
Methodof Continuous Variation: Characterization ofAlkali Metal Enolates Using 1H and 19F NMR Spectroscopies
Linear Mode
