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B Stec

Showing results (21-30 of 36) with videos related to

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Journal of Protein Chemistry|February 1, 1990
Crystallization of alcohol oxidase from Pichia pastoris. Secondary structure predictions indicate a domain with the eightfold beta/alpha-barrel foldE Tykarska, L Lebioda, E Marchut, et al.
Nature Structural Biology|August 1, 1997
Trapping and visualization of a covalent enzyme-phosphate intermediateJ E Murphy, B Stec, L Ma, et al.
Protein Science : a Publication of the Protein Society|November 1, 1996
Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativityG Lu, B Stec, E L Giroux, et al.
Proteins|January 29, 2000
Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 AL Jin, B Stec, W N Lipscomb, et al.
Nature Structural Biology|April 27, 2001
Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylaseC P Macol, H Tsuruta, B Stec, et al.
Journal of Medicinal Chemistry|September 2, 1994
Homology modeling of the dopamine D2 receptor and its testing by docking of agonists and tricyclic antagonistsM M Teeter, M Froimowitz, B Stec, et al.
Protein Science : a Publication of the Protein Society|July 1, 1999
The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativityC Macol, M Dutta, B Stec, et al.
Biochemistry|February 15, 2001
Crystal structure and catalytic mechanism of the MJ0109 gene product: a bifunctional enzyme with inositol monophosphatase and fructose 1,6-bisphosphatase activitiesK A Johnson, L Chen, H Yang, et al.
Nature Structural Biology|November 4, 2000
MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphataseB Stec, H Yang, K A Johnson, et al.
Journal of Molecular Biology|May 23, 1998
Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102B Stec, M J Hehir, C Brennan, et al.
Pageof 4

Showing results (21-30 of 36) with videos related to

Sort By:
Pageof 4
Journal of Protein Chemistry|February 1, 1990
Crystallization of alcohol oxidase from Pichia pastoris. Secondary structure predictions indicate a domain with the eightfold beta/alpha-barrel foldE Tykarska, L Lebioda, E Marchut, et al.
Nature Structural Biology|August 1, 1997
Trapping and visualization of a covalent enzyme-phosphate intermediateJ E Murphy, B Stec, L Ma, et al.
Protein Science : a Publication of the Protein Society|November 1, 1996
Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativityG Lu, B Stec, E L Giroux, et al.
Proteins|January 29, 2000
Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 AL Jin, B Stec, W N Lipscomb, et al.
Nature Structural Biology|April 27, 2001
Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylaseC P Macol, H Tsuruta, B Stec, et al.
Journal of Medicinal Chemistry|September 2, 1994
Homology modeling of the dopamine D2 receptor and its testing by docking of agonists and tricyclic antagonistsM M Teeter, M Froimowitz, B Stec, et al.
Protein Science : a Publication of the Protein Society|July 1, 1999
The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativityC Macol, M Dutta, B Stec, et al.
Biochemistry|February 15, 2001
Crystal structure and catalytic mechanism of the MJ0109 gene product: a bifunctional enzyme with inositol monophosphatase and fructose 1,6-bisphosphatase activitiesK A Johnson, L Chen, H Yang, et al.
Nature Structural Biology|November 4, 2000
MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphataseB Stec, H Yang, K A Johnson, et al.
Journal of Molecular Biology|May 23, 1998
Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102B Stec, M J Hehir, C Brennan, et al.
Pageof 4