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Biochemistry|February 10, 1998
The C-terminal half of the anti-sigma factor FlgM contains a dynamic equilibrium solution structure favoring helical conformationsG W Daughdrill, L J Hanely, F W DahlquistIET Systems Biology|August 22, 2007
Simultaneous high gain and wide dynamic range in a model of bacterial chemotaxisM-J Park, F W Dahlquist, F J DoyleJournal of Bacteriology|June 1, 1990
Mutations that affect control of the methylesterase activity of CheB, a component of the chemotaxis adaptation system in Escherichia coliR C Stewart, A F Roth, F W DahlquistBiochemistry|September 14, 1982
Fluorinated ligands as nuclear magnetic resonance probes of active-site nonequivalence in abortive ternary complexes of horse liver alcohol dehydrogenaseD C Anderson, M L Wilson, F W DahlquistJournal of Bacteriology|January 1, 1985
Aberrant regulation of methylesterase activity in cheD chemotaxis mutants of Escherichia coliM R Kehry, T G Doak, F W DahlquistProtein Science : a Publication of the Protein Society|September 23, 1997
Determination of pKa values of the histidine side chains of phosphatidylinositol-specific phospholipase C from Bacillus cereus by NMR spectroscopy and site-directed mutagenesisT Liu, M Ryan, F W Dahlquist, et al.Biochemistry|October 5, 2001
A catalytic diad involved in substrate-assisted catalysis: NMR study of hydrogen bonding and dynamics at the active site of phosphatidylinositol-specific phospholipase CM Ryan, T Liu, F W Dahlquist, et al.Journal of Molecular Biology|June 22, 1999
Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein fliMM M McEvoy, A Bren, M Eisenbach, et al.Biochemistry|May 26, 1981
Dynamical and temperature-dependent effects of lipid-protein interactions. Application of deuterium nuclear magnetic resonance and electron paramagnetic resonance spectroscopy to the same reconstitutions of cytochrome c oxidaseM R Paddy, F W Dahlquist, J H Davis, et al.Biochemistry|September 1, 1992
Protein folding: assignment of the energetic changes of reversible chemical modifications to the folded or unfolded statesJ Lu, W A Baase, D C Muchmore, et al.Pageof 11