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Jack F Kirsch

Showing results (11-20 of 40) with videos related to

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Accounts of Chemical Research|October 22, 2003
Avoiding the road less traveled: how the topology of enzyme-substrate complexes can dictate product selectionAndrew C Eliot, Jack F Kirsch
Journal of Molecular Biology|March 14, 2003
How does an enzyme evolved in vitro compare to naturally occurring homologs possessing the targeted function? Tyrosine aminotransferase from aspartate aminotransferaseSteven C Rothman, Jack F Kirsch
Biochemistry|December 23, 2008
The partially folded homodimeric intermediate of Escherichia coli aspartate aminotransferase contains a "molten interface" structureEdgar Deu, Jashdeep Dhoot, Jack F Kirsch
Archives of Biochemistry and Biophysics|December 18, 2003
S-methylmethionine is both a substrate and an inactivator of 1-aminocyclopropane-1-carboxylate synthaseSaeHee Ko, Andrew C Eliot, Jack F Kirsch
Protein Science : a Publication of the Protein Society|September 19, 2002
How do two unrelated antibodies, HyHEL-10 and F9.13.7, recognize the same epitope of hen egg-white lysozyme?Jaume Pons, Jennifer R Stratton, Jack F Kirsch
Protein Science : a Publication of the Protein Society|February 10, 2004
Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferaseSteven C Rothman, Mark Voorhies, Jack F Kirsch
Protein Science : a Publication of the Protein Society|April 23, 2002
The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: multiple forced covariant amino acid substitutions in natural variantsEdgar Deu, Keith A Koch, Jack F Kirsch
Biochemistry|September 25, 2003
Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for the elimination and substitution reactionsSusan M Aitken, Daniel H Kim, Jack F Kirsch
Protein Science : a Publication of the Protein Society|May 30, 2006
Free energies of protein-protein association determined by electrospray ionization mass spectrometry correlate accurately with values obtained by solution methodsSanjay R Krishnaswamy, Evan R Williams, Jack F Kirsch
Biochemistry|October 16, 2002
The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutationAndrew C Eliot, Jenny Sandmark, Gunter Schneider, et al.
Pageof 4

Showing results (11-20 of 40) with videos related to

Sort By:
Pageof 4
Accounts of Chemical Research|October 22, 2003
Avoiding the road less traveled: how the topology of enzyme-substrate complexes can dictate product selectionAndrew C Eliot, Jack F Kirsch
Journal of Molecular Biology|March 14, 2003
How does an enzyme evolved in vitro compare to naturally occurring homologs possessing the targeted function? Tyrosine aminotransferase from aspartate aminotransferaseSteven C Rothman, Jack F Kirsch
Biochemistry|December 23, 2008
The partially folded homodimeric intermediate of Escherichia coli aspartate aminotransferase contains a "molten interface" structureEdgar Deu, Jashdeep Dhoot, Jack F Kirsch
Archives of Biochemistry and Biophysics|December 18, 2003
S-methylmethionine is both a substrate and an inactivator of 1-aminocyclopropane-1-carboxylate synthaseSaeHee Ko, Andrew C Eliot, Jack F Kirsch
Protein Science : a Publication of the Protein Society|September 19, 2002
How do two unrelated antibodies, HyHEL-10 and F9.13.7, recognize the same epitope of hen egg-white lysozyme?Jaume Pons, Jennifer R Stratton, Jack F Kirsch
Protein Science : a Publication of the Protein Society|February 10, 2004
Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferaseSteven C Rothman, Mark Voorhies, Jack F Kirsch
Protein Science : a Publication of the Protein Society|April 23, 2002
The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: multiple forced covariant amino acid substitutions in natural variantsEdgar Deu, Keith A Koch, Jack F Kirsch
Biochemistry|September 25, 2003
Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for the elimination and substitution reactionsSusan M Aitken, Daniel H Kim, Jack F Kirsch
Protein Science : a Publication of the Protein Society|May 30, 2006
Free energies of protein-protein association determined by electrospray ionization mass spectrometry correlate accurately with values obtained by solution methodsSanjay R Krishnaswamy, Evan R Williams, Jack F Kirsch
Biochemistry|October 16, 2002
The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutationAndrew C Eliot, Jenny Sandmark, Gunter Schneider, et al.
Pageof 4