Quantifying the limits of transition state theory in enzymatic catalysis.

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Quantifying the limits of transition state theory in enzymatic catalysis.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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Quantifying the limits of transition state theory in enzymatic catalysis.

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Quantifying the limits of transition state theory in enzymatic catalysis.

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Quantifying the limits of transition state theory in enzymatic catalysis.

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Quantifying the limits of transition state theory in enzymatic catalysis.

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Quantifying the limits of transition state theory in enzymatic catalysis.

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Quantifying the limits of transition state theory in enzymatic catalysis.

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P1476

Quantifying the limits of transition state theory in enzymatic catalysis.

@en

P2093

Kirill Zinovjev

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P2860

A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis

Comparison of simple potential functions for simulating liquid water

Development and use of quantum mechanical molecular models. 76. AM1: a new general purpose quantum mechanical molecular model

Intrinsic motions along an enzymatic reaction trajectory

Divergent evolution of protein conformational dynamics in dihydrofolate reductase.

The mechanism of cellulose hydrolysis by a two-step, retaining cellobiohydrolase elucidated by structural and transition path sampling studies

How enzymes work: analysis by modern rate theory and computer simulations

At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?

Chemical Ligation and Isotope Labeling to Locate Dynamic Effects during Catalysis by Dihydrofolate Reductase

Perspective: Defining and quantifying the role of dynamics in enzyme catalysis

P304

12390-12395

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P31

scholarly article

P356

10.1073/PNAS.1710820114

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P407

English

P433

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P478

114

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P50

Iñaki Tuñón

P577

2017-11-03T00:00:00Z

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P698

29101125

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P932

5703300

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