Chemical Ligation and Isotope Labeling to Locate Dynamic Effects during Catalysis by Dihydrofolate Reductase - sprookjes - yvandenbroek - TriplyDB

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

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

http://www.wikidata.org/entity/Q28830226

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Triple Isotope Effects Support Concerted Hydride and Proton Transfer and Promoting Vibrations in Human Heart Lactate Dehydrogenase Hydride Transfer in DHFR by Transition Path Sampling, Kinetic Isotope Effects, and Heavy Enzyme Studies A complete thermodynamic analysis of enzyme turnover links the free energy landscape to enzyme catalysis.Dynamic and Electrostatic Effects on the Reaction Catalyzed by HIV-1 Protease.Aligator: A computational tool for optimizing total chemical synthesis of large proteins.Pinpointing dynamic coupling in enzymes for efficient drug design.Quantifying the limits of transition state theory in enzymatic catalysis.Protonation-Initiated Cyclization by a Class II Terpene Cyclase Assisted by Tunneling.Minimization of dynamic effects in the evolution of dihydrofolate reductase† †Electronic supplementary information (ESI) available: Full experimental procedures; mass spectra of purified proteins; circular dichroism spectra, tabulated experimental d

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

http://www.wikidata.org/entity/Q28830226

description

2015 nî lūn-bûn

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2015 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2015 թվականի հուլիսին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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Chemical Ligation and Isotope ...... sis by Dihydrofolate Reductase

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Chemical Ligation and Isotope ...... sis by Dihydrofolate Reductase

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Chemical Ligation and Isotope ...... sis by Dihydrofolate Reductase

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Chemical Ligation and Isotope ...... sis by Dihydrofolate Reductase

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Angewandte Chemie International Edition

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Chemical Ligation and Isotope ...... sis by Dihydrofolate Reductase

@en

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Aduragbemi S Adesina

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Rudolf K Allemann

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P2860

Network of coupled promoting motions in enzyme catalysis

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

Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence

A new conceptual framework for enzyme catalysis. Hydrogen tunnelling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes

The dynamic energy landscape of dihydrofolate reductase catalysis

Synthesis of proteins by native chemical ligation

A new conceptual framework for enzyme catalysis

Effects of a distal mutation on active site chemistry.

Enzyme millisecond conformational dynamics do not catalyze the chemical step.

Enzymatic H-transfer requires vibration-driven extreme tunneling.

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9016-9020

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scholarly article

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10.1002/ANIE.201503968

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31

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54

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J Javier Ruiz-Pernía

E Joel Loveridge

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2015-06-16T00:00:00Z

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278731383

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26079622

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isotopic labeling

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4985705

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