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The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer.


ABSTRACT: 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.

SUBMITTER: Stojkovic V 

PROVIDER: S-EPMC4346287 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature

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The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer.

Stojković Vanja V   Perissinotti Laura L LL   Lee Jeeyeon J   Benkovic Stephen J SJ   Kohen Amnon A  

Chemical communications (Cambridge, England) 20101025 47


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. ...[more]

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