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4-nitrophenylgalactoside and serine

4-nitrophenylgalactoside has been researched along with serine in 1 studies

Research

Studies (1)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	1 (100.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Fraser, ME; Huber, RE; Jancewicz, LJ; Lee, M; Sutendra, G; Wheatley, RW	1

Other Studies

1 other study(ies) available for 4-nitrophenylgalactoside and serine

Article	Year
Ser-796 of β-galactosidase (Escherichia coli) plays a key role in maintaining a balance between the opened and closed conformations of the catalytically important active site loop. Archives of biochemistry and biophysics, 2012, Jan-15, Volume: 517, Issue:2 Topics: Amino Acid Substitution; beta-Galactosidase; Catalytic Domain; Crystallography, X-Ray; Enzyme Inhibitors; Escherichia coli; Escherichia coli Proteins; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Isopropyl Thiogalactoside; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Protein Conformation; Recombinant Proteins; Serine; Static Electricity	2012

Article

Year

Ser-796 of β-galactosidase (Escherichia coli) plays a key role in maintaining a balance between the opened and closed conformations of the catalytically important active site loop.

Archives of biochemistry and biophysics, 2012, Jan-15, Volume: 517, Issue:2

Topics: Amino Acid Substitution; beta-Galactosidase; Catalytic Domain; Crystallography, X-Ray; Enzyme Inhibitors; Escherichia coli; Escherichia coli Proteins; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Isopropyl Thiogalactoside; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Protein Conformation; Recombinant Proteins; Serine; Static Electricity

2012