<p>Substrate B is yields products C and D with a release of free energy ER. Although the overall reaction is thermodynamically favorable, there is an energy barrier (the activation energy [Ea]) that decreases the rate of the reaction (k). The enzyme, through a key-lock geometric binding with the substrate, has a net effect of reducing the Ea and accelerating the reaction. As described in the text, the information content of the enzyme is expressed geometrically by the formation of a shape within the protein that is precisely complementary to the shape of the substrate. The information is, thus, converted to energy by reducing Ea (ΔEa).</p
<p>An enzyme with a characteristic rate k<sub>1</sub> is trapped in a local minimum. When a heat pul...
Kinetic models provide the means to understand and predict the dynamic behaviour of en-zymes upon di...
Why are enzyme-catalyzed reactions so much faster than uncatalyzed reactions, and why are enzymes so...
The reaction rate enhancement that enzymes produce had not been fully appreciated. The object of the...
<p>(A) Hypothetical uncatalyzed reaction profile. (B) Hypothetical enzyme that stabilizes the ground...
<p>(A) Schematic representation of the bimolecular mechanisms considered for the analysis. (B) Subst...
<p>The left panel illustrates the Michaelis-Menten scheme of Equation (8), in which enzyme binds to ...
Despite advances in computational design of protein structures, it has proven very difficult to desi...
Enzymes are proteins that accelerate intracellular chemical reactions often by factors of 10(5) - 10...
<p><b>A.</b> Thermodynamic cycle relating the energy of the cyclization reaction in solution with th...
Advances in transition state theory and computer simulations are providing new insights into the sou...
<p>E, S, and P stand for enzyme, substrates, and products; the upper branch refers to the forward re...
Abstract: An energy decomposition scheme is presented to elucidate the importance of the change of ...
Elucidating the relationship between the free energy landscape of enzymes and their catalytic power ...
AbstractThe mechanism by which enzymes produce enormous rate enhancements in the reactions they cata...
<p>An enzyme with a characteristic rate k<sub>1</sub> is trapped in a local minimum. When a heat pul...
Kinetic models provide the means to understand and predict the dynamic behaviour of en-zymes upon di...
Why are enzyme-catalyzed reactions so much faster than uncatalyzed reactions, and why are enzymes so...
The reaction rate enhancement that enzymes produce had not been fully appreciated. The object of the...
<p>(A) Hypothetical uncatalyzed reaction profile. (B) Hypothetical enzyme that stabilizes the ground...
<p>(A) Schematic representation of the bimolecular mechanisms considered for the analysis. (B) Subst...
<p>The left panel illustrates the Michaelis-Menten scheme of Equation (8), in which enzyme binds to ...
Despite advances in computational design of protein structures, it has proven very difficult to desi...
Enzymes are proteins that accelerate intracellular chemical reactions often by factors of 10(5) - 10...
<p><b>A.</b> Thermodynamic cycle relating the energy of the cyclization reaction in solution with th...
Advances in transition state theory and computer simulations are providing new insights into the sou...
<p>E, S, and P stand for enzyme, substrates, and products; the upper branch refers to the forward re...
Abstract: An energy decomposition scheme is presented to elucidate the importance of the change of ...
Elucidating the relationship between the free energy landscape of enzymes and their catalytic power ...
AbstractThe mechanism by which enzymes produce enormous rate enhancements in the reactions they cata...
<p>An enzyme with a characteristic rate k<sub>1</sub> is trapped in a local minimum. When a heat pul...
Kinetic models provide the means to understand and predict the dynamic behaviour of en-zymes upon di...
Why are enzyme-catalyzed reactions so much faster than uncatalyzed reactions, and why are enzymes so...