ShereKhan - Calculating exchange parameters in relaxation dispersion data from CPMG experiments

Bioinformatics

Volumn 29, Issue 14, 2013, Pages 1819-1820

  Mazur, Adam ^a   Hammesfahr, Björn ^a   Griesinger, Christian ^a   Lee, Donghan ^a   Kollmar, Martin ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; COMPUTER PROGRAM; INTERNET; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE; PROCEDURES;

INTERNET; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; SOFTWARE;

EID: 84880192817     PISSN: 13674803     EISSN: 14602059     Source Type: Journal    
DOI: 10.1093/bioinformatics/btt286     Document Type: Article

References (12)

1. Ban, D. et al. (2012) Exceeding the limit of dynamics studies on biomolecules using high spin-lock field strengths with a cryogenically cooled probehead. J. Magn. Reson., 221, 1-4.
2. Bieri, M. and Gooley, P.R. (2011) Automated NMR relaxation dispersion data analysis using NESSY. BMC Bioinformatics, 12, 421.
3. Bostock, M. and Heer, J. (2009) Protovis: a graphical toolkit for visualization. IEEE Trans. Vis. Comput. Graph., 15, 1121-1128.
4. Carver, J. and Richards, R. (1972) General 2-site solution for chemical exchange produced dependence of T2 upon Carr-Purcell pulse separation. J. Magn. Reson., 6, 89-96.
5. Davis, D.G. et al. (1994) Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1 rho and T2 (CPMG) methods. J. Magn. Reson. B, 104, 266-275.
6. Kleckner, I.R. and Foster, M.P. (2012) GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data. J. Biomol. NMR, 52, 11-22.
7. Luz, Z. and Meiboom, S. (1963) Nuclear magnetic resonance study of the protolysis of trimethylammonium ion in aqueous solution-order of the reaction with respect to solvent. J. Chem. Phys., 39, 366-370.
8. McConnell, H.M. (1958) Reaction rates by nuclear magnetic resonance. J. Chem. Phys., 28, 430-431.
9. Millet, O. et al. (2000) The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale. J. Am. Chem. Soc., 122, 2867-2877.
10. Mittermaier, A. and Kay, L.E. (2006) New tools provide new insights in NMR studies of protein dynamics. Science, 312, 224-228.
11. Mulder, F.A. et al. (2001) Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme. J. Am. Chem. Soc., 123, 967-975.
12. Wang, C. et al. (2001) CPMG sequences with enhanced sensitivity to chemical exchange. J. Biomol. NMR, 21, 361-366.