Related ArticlesFactors determining the reliable description of global tumbling parameters in solution NMR.
J Biomol NMR. 2002 Nov;24(3):215-29
Authors: Pawley NH, Gans JD, Nicholson LK
An accurate description of global tumbling of a protein is essential for correct analysis and interpretation of internal dynamics and thermodynamics. The accurate fitting of global tumbling parameters is affected by the number of experimental relaxation data points available for analysis, the distribution of data points over the domain of the function describing the tumbling, the measurement error associated with the data, the error associated with use of an approximate functional form, and errors in the protein structure. We present an analysis of the influence of these factors on the error in global tumbling parameters and the corresponding error in the calculated T(1)/T(2) values. We find that reduction of experimental and approximation error can compensate for a less-than-ideal quantity or distribution of data points, and that accurate parameters can be obtained for proteins with highly anisotropic distributions of bond vectors, as illustrated using the helical bundle protein G-CSF. This indicates that proteins with anisotropic distributions, such as the helical bundle class of proteins, should not summarily be excluded when selecting proteins for dynamic and thermodynamic analyses of (15)N backbone relaxation measurements.
News relating to impact factors
News relating to impact factors
News relating to impact factors
Content Type Journal Article
Category Editorial
Pages 1-1
DOI 10.1007/s10858-011-9557-6
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A DOTA-amide lanthanide tag for reliable generation of pseudocontact shifts in protein NMR spectra.
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Bioconjug Chem. 2011 Aug 31;
Authors: Graham B, Loh CT, Swarbrick JD, Ung P, Shin J, Yagi H, Jia X, Chhabra S, Barlow N, Pintacuda G, Huber T, Otting G
Abstract
Structural studies of proteins and protein-ligand complexes by nuclear magnetic resonance (NMR) spectroscopy can be greatly enhanced by site-specific attachment of lanthanide ions to...
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09-01-2011 05:20 PM
[NMR paper] More reliable protein NMR peak assignment via improved 2-interval scheduling.
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J Comput Biol. 2005 Mar;12(2):129-46
Authors: Chen ZZ, Lin G, Rizzi R, Wen J, Xu D, Xu Y, Jiang T
Protein NMR peak assignment refers to the process of assigning a group of "spin systems" obtained experimentally to a protein sequence of amino acids. The automation of this process is still an unsolved and challenging problem in NMR protein structure determination. Recently,...
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11-24-2010 11:14 PM
[NMR paper] Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solutio
Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR.
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Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3409-13
Authors: Klein-Seetharaman J, Yanamala NV, Javeed F, Reeves PJ, Getmanova EV, Loewen MC, Schwalbe H, Khorana HG
G protein-coupled receptors are cell-surface seven-helical membrane proteins that undergo conformational changes on activation. The mammalian photoreceptor, rhodopsin, is the...
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11-24-2010 09:25 PM
[NMR paper] A general NMR method for rapid, efficient, and reliable biochemical screening.
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J Am Chem Soc. 2003 Nov 26;125(47):14620-5
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High-throughput screening is usually the method of drug-lead discovery. It is now well accepted that, for a functional assay, quality is more important than quantity. The ligand-based or protein-based NMR screening methodologies for detecting compounds...
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11-24-2010 09:16 PM
[NMR paper] Three-dimensional structure of the FK506 binding protein/ascomycin complex in solutio
Three-dimensional structure of the FK506 binding protein/ascomycin complex in solution by heteronuclear three- and four-dimensional NMR.
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Biochemistry. 1993 Jan 26;32(3):754-65
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A high-resolution three-dimensional solution structure of the FKBP/ascomycin complex has been...
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[NMR paper] NMR studies in experimental allergic encephalomyelitis: factors which contribute to T
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Magn Reson Med. 1990 Apr;14(1):1-11
Authors: Karlik SJ, Gilbert JJ, Wong C, Vandervoort MK, Noseworthy JH
To determine the factors which may alter NMR relaxation times in multiple sclerosis (MS) lesions we measured the proton T1 and T2, specific gravity (SG), and histology in the central nervous system (CNS; 13-19 levels per...
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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.
Factors determining the reliable description of global tumbling parameters in solutio
Linear Mode
