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Journal of Molecular Biology|March 5, 1990
Detergent-solubilized M13 coat protein exists as an asymmetric dimer. Observation of individual monomers by 15N, 13C and 1H nuclear magnetic resonance spectroscopyG D Henry, B D SykesMethods in Enzymology|January 1, 1994
Methods to study membrane protein structure in solutionG D Henry, B D SykesBiochemistry and Cell Biology = Biochimie Et Biologie Cellulaire|March 1, 1994
A nuclear magnetic resonance study of the DNA-binding affinity of Cro repressor protein stabilized by a disulfide bondJ D Baleja, B D SykesJournal of Biomolecular NMR|August 23, 2012
Determination of the rotational dynamics and pH dependence of the hydrogen exchange rates of the arginine guanidino group using NMR spectroscopyG D Henry, B D SykesThe Journal of Biological Chemistry|March 10, 1975
Concanavalin A: a stopped flow nuclear magnetic resonance study of conformational changes induced by Mn++, Ca++, and alpha-methyl-D-mannosideJ J Grimaldi, B D SykesBiochemistry|April 19, 1988
Structure and dynamics of a detergent-solubilized membrane protein: measurement of amide hydrogen exchange rates in M13 coat protein by 1H NMR spectroscopyJ D O'Neil, B D SykesCanadian Journal of Biochemistry|September 1, 1982
In situ enzymatic removal of orthophosphate by the nucleoside phosphorylase catalyzed phosphorolysis of nicotinamide ribosideJ W Shriver, B D SykesJournal of Biomolecular NMR|March 1, 1994
The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift dataD S Wishart, B D SykesBiochemistry and Cell Biology = Biochimie Et Biologie Cellulaire|January 1, 1990
Structure and dynamics of detergent-solubilized M13 coat protein (an integral membrane protein) determined by 13C and 15N nuclear magnetic resonance spectroscopyG D Henry, B D SykesBiochemistry|April 6, 1993
1H-NMR resonance assignments, secondary structure, and global fold of the TR1C fragment of turkey skeletal troponin C in the calcium-free stateW A Findlay, B D SykesPageof 95