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Acta Crystallographica. Section D, Biological Crystallography|November 28, 2000
A systematic case study on using NMR models for molecular replacement: p53 tetramerization domain revisitedY W Chen, G M CloreProceedings of the National Academy of Sciences of the United States of America|August 2, 2000
Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear overhauser enhancement data and dipolar couplings by rigid body minimizationG M CloreBiochimica Et Biophysica Acta|January 14, 1981
A re-evaluation of the low-temperature kinetics of the reaction of fully reduced mitochondrial cytochrome oxidase with carbon monoxide and the spectral characterization of species Ic in the Soret and visible regionsG M CloreBiochimica Et Biophysica Acta|March 15, 1979
A temperature-induced absorption band centered in the region of 666 nm related to the configuration of the active site in frozen cytochrome oxidaseM Denis, G M CloreJournal of Magnetic Resonance (San Diego, Calif. : 1997)|September 26, 2000
Sources of and solutions to problems in the refinement of protein NMR structures against torsion angle potentials of mean forceJ Kuszewski, G M CloreJournal of Magnetic Resonance (San Diego, Calif. : 1997)|July 30, 2021
The measurement of relaxation rates of degenerate 1H transitions in methyl groups of proteins using acute angle radiofrequency pulsesV Tugarinov, G M ClorePlant Physiology|July 1, 1981
Reaction of Mixed Valence State Cytochrome Oxidase with Oxygen in Plant Mitochondria: A STUDY BY LOW TEMPERATURE FLASH PHOTOLYSIS AND RAPID WAVELENGTH SCANNING OPTICAL SPECTROMETRYM Denis, G M CloreEuropean Biophysics Journal : EBJ|January 1, 1984
An investigation into the solution structure of the single-stranded DNA undecamer 5'd AAGTGTGATAT by means of nuclear Overhauser enhancement measurementsG M Clore, A M GronenbornScience (New York, N.Y.)|June 7, 1991
Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopyG M Clore, A M GronenbornPageof 48