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Shamina Hakda

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Biochemistry|November 19, 2003
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidaseDouglas H Juers, Shamina Hakda, Brian W Matthews, et al.
Cryobiology|August 5, 2008
A non-ideal replacement for the Boyle van't Hoff equationRichelle C Prickett, Janet A W Elliott, Shamina Hakda, et al.
Biochemistry|February 13, 2003
Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducerReuben E Huber, Shamina Hakda, Calvino Cheng, et al.
Pageof 1

Showing results (1-10 of 3) with videos related to

Sort By:
Pageof 1
Biochemistry|November 19, 2003
Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidaseDouglas H Juers, Shamina Hakda, Brian W Matthews, et al.
Cryobiology|August 5, 2008
A non-ideal replacement for the Boyle van't Hoff equationRichelle C Prickett, Janet A W Elliott, Shamina Hakda, et al.
Biochemistry|February 13, 2003
Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducerReuben E Huber, Shamina Hakda, Calvino Cheng, et al.
Pageof 1