<p>(A) The kinetic scheme for the interaction of substrate with a two-state handle region, where the open state is the binding-competent state. (B) The kinetic scheme for a single-state handle region, in which the loop is held in a single conformation well-positioned for substrate interactions.</p
AbstractThermodynamic measurements of proteins indicate that the folding to the native state takes p...
There has been much interest in understanding the rates of protein folding in terms of transitionsta...
Biomolecular recognition often involves large conformational changes, sometimes even local unfolding...
<p>The kinetic scheme describing the interactions of APE1K98A with specific F- and AP-substrates dur...
Many proteins exhibit multiple binding patches. A patch may harbour a key chemical modification site...
<p>The kinetic scheme describing the interactions of APE1K98A with specific DHU-substrate during NIR...
<p>The kinetic scheme describing the interactions of APE1K98A with undamaged ligand.</p
The discerning behavior of living systems relies on accurate interactions selected from the lot of m...
Understanding the kinetic behavior of complex systems is crucial for the study of physical, chemical...
<p>IDE<sub>C</sub> and IDE<sub>O</sub> represent the closed and open conformations of IDE respectful...
To clarify the interplay between the binding affinity and kinetics of protein-protein interactions, ...
The kinetic modelling of biochemical pathways requires a consistent set of enzymatic kinetic paramet...
<div><p>The kinetic rate constants of binding were estimated for four biochemically relevant molecul...
<p>One-step binding: the inhibitor [I] and substrate [S] are in equilibrium; binding is competitive ...
We study the nature of biomolecular binding. We found that in general there exists several thermodyn...
AbstractThermodynamic measurements of proteins indicate that the folding to the native state takes p...
There has been much interest in understanding the rates of protein folding in terms of transitionsta...
Biomolecular recognition often involves large conformational changes, sometimes even local unfolding...
<p>The kinetic scheme describing the interactions of APE1K98A with specific F- and AP-substrates dur...
Many proteins exhibit multiple binding patches. A patch may harbour a key chemical modification site...
<p>The kinetic scheme describing the interactions of APE1K98A with specific DHU-substrate during NIR...
<p>The kinetic scheme describing the interactions of APE1K98A with undamaged ligand.</p
The discerning behavior of living systems relies on accurate interactions selected from the lot of m...
Understanding the kinetic behavior of complex systems is crucial for the study of physical, chemical...
<p>IDE<sub>C</sub> and IDE<sub>O</sub> represent the closed and open conformations of IDE respectful...
To clarify the interplay between the binding affinity and kinetics of protein-protein interactions, ...
The kinetic modelling of biochemical pathways requires a consistent set of enzymatic kinetic paramet...
<div><p>The kinetic rate constants of binding were estimated for four biochemically relevant molecul...
<p>One-step binding: the inhibitor [I] and substrate [S] are in equilibrium; binding is competitive ...
We study the nature of biomolecular binding. We found that in general there exists several thermodyn...
AbstractThermodynamic measurements of proteins indicate that the folding to the native state takes p...
There has been much interest in understanding the rates of protein folding in terms of transitionsta...
Biomolecular recognition often involves large conformational changes, sometimes even local unfolding...
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