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FEBS Letters|July 9, 1984
Internal mobility in a double-stranded B DNA hexamer and undecamer. A time-dependent proton-proton nuclear Overhauser enhancement studyG M Clore, A M GronenbornThe Biochemical Journal|February 1, 1979
Low-temperature kinetics of the reactions of fully reduced membrane-bound cytochrome oxidase with oxygen in the Soret, alpha and near-infrared regionsG M Clore, E M ChanceJournal of Magnetic Resonance (San Diego, Calif. : 1997)|March 4, 2000
Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation timesG Kontaxis, G M Clore, A BaxThe Journal of Biological Chemistry|October 25, 2000
A novel membrane anchor function for the N-terminal amphipathic sequence of the signal-transducing protein IIAGlucose of the Escherichia coli phosphotransferase systemG Wang, A Peterkofsky, G M CloreJournal of the American Chemical Society|July 18, 2001
Improving the accuracy of NMR structures of DNA by means of a database potential of mean force describing base-base positional interactionsJ Kuszewski, C Schwieters, G M CloreJournal of Magnetic Resonance (San Diego, Calif. : 1997)|January 29, 2000
Direct refinement against proton-proton dipolar couplings in NMR structure determination of macromoleculesN Tjandra, J Marquardt, G M CloreFEBS Letters|March 14, 1988
Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculationsM Nilges, G M Clore, A M GronenbornJournal of Magnetic Resonance (San Diego, Calif. : 1997)|July 9, 1998
A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural informationG M Clore, A M Gronenborn, A BaxJournal of Biomolecular NMR|May 1, 1991
Stereospecific assignment of beta-methylene protons in larger proteins using 3D 15N-separated Hartmann-Hahn and 13C-separated rotating frame Overhauser spectroscopyG M Clore, A Bax, A M GronenbornProtein Science : a Publication of the Protein Society|June 1, 1996
Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databasesJ Kuszewski, A M Gronenborn, G M ClorePageof 48