Electrostatic basis for enzyme catalysis
Enzymatic reactions play a fundamentally important role in controlling and performing most
life processes. 1-3 Thus, understanding how enzymes work has both fundamental and …
life processes. 1-3 Thus, understanding how enzymes work has both fundamental and …
How enzymes work: analysis by modern rate theory and computer simulations
M Garcia-Viloca, J Gao, M Karplus, DG Truhlar - Science, 2004 - science.org
Advances in transition state theory and computer simulations are providing new insights into
the sources of enzyme catalysis. Both lowering of the activation free energy and changes in …
the sources of enzyme catalysis. Both lowering of the activation free energy and changes in …
A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis
Conformational dynamics play a key role in enzyme catalysis. Although protein motions
have clear implications for ligand flux, a role for dynamics in the chemical step of enzyme …
have clear implications for ligand flux, a role for dynamics in the chemical step of enzyme …
Conformational selection or induced fit: a flux description of reaction mechanism
The mechanism of ligand binding coupled to conformational changes in macromolecules
has recently attracted considerable interest. The 2 limiting cases are the “induced fit” …
has recently attracted considerable interest. The 2 limiting cases are the “induced fit” …
[HTML][HTML] A general chemical method to regulate protein stability in the mammalian central nervous system
M Iwamoto, T Björklund, C Lundberg, D Kirik… - Chemistry & biology, 2010 - cell.com
The ability to make specific perturbations to biological molecules in a cell or organism is a
central experimental strategy in modern research biology. We have developed a general …
central experimental strategy in modern research biology. We have developed a general …
Allosteric regulation and catalysis emerge via a common route
NM Goodey, SJ Benkovic - Nature chemical biology, 2008 - nature.com
Allosteric regulation of protein function is a mechanism by which an event in one place of a
protein structure causes an effect at another site, much like the behavior of a …
protein structure causes an effect at another site, much like the behavior of a …
Structure, dynamics, and catalytic function of dihydrofolate reductase
JR Schnell, HJ Dyson, PE Wright - Annu. Rev. Biophys. Biomol …, 2004 - annualreviews.org
▪ Abstract Molecular motions are widely regarded as contributing factors in many aspects of
protein function. The enzyme dihydrofolate reductase (DHFR), and particularly that from …
protein function. The enzyme dihydrofolate reductase (DHFR), and particularly that from …
An NMR perspective on enzyme dynamics
DD Boehr, HJ Dyson, PE Wright - Chemical reviews, 2006 - ACS Publications
Enzyme catalysis is an inherently dynamic process. Binding and release of ligands is often
accompanied by conformational changes, both subtle and dramatic (reviewed more …
accompanied by conformational changes, both subtle and dramatic (reviewed more …
[图书][B] Isotope effects in chemistry and biology
A Kohen, HH Limbach - 2005 - taylorfrancis.com
The field of isotope effects has expanded exponentially in the last decade, and researchers
are finding isotopes increasingly useful in their studies. Bringing literature on the subject up …
are finding isotopes increasingly useful in their studies. Bringing literature on the subject up …
Interaction of dihydrofolate reductase with methotrexate: ensemble and single-molecule kinetics
PTR Rajagopalan, Z Zhang… - Proceedings of the …, 2002 - National Acad Sciences
The thermodynamics and kinetics of the interaction of dihydrofolate reductase (DHFR) with
methotrexate have been studied by using fluorescence, stopped-flow, and single-molecule …
methotrexate have been studied by using fluorescence, stopped-flow, and single-molecule …