The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer
Comparison of the nature of hydride transfer in wild-type and active site mutant (I14A) of dihydrofolate reductase suggests that the size of this side chain at position 14 modulates H-tunneling. © 2010 The Royal Society of Chemistry.
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2010
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13597345_v46_n47_p8974_Stojković http://hdl.handle.net/20.500.12110/paper_13597345_v46_n47_p8974_Stojković |
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