<p>Δ<sup>i</sup>G indicates the solvation free energy gain upon formation of the interface and negative value corresponds to positive protein affinity.</p><p>Interaction energies (Δ<sup>i</sup>G) of native and mutant forms of KFG-KITLG docked complex.</p
AbstractWe report the computer generation of a high-density map of the thermodynamic properties of t...
Protein recognition is one of the most challenging and intriguing pro-blems in structural biology. D...
Protein-protein complexes orchestrate most cellular processes such as transcription, signal transduc...
<p>Interaction energy and interface Accessible Surface Area (ASA) in the minimized complexes emergin...
<p>Free energy estimated for noncovalent interactions involving active site residues Q39 and E451 an...
In the crowded cell, the competition between functional and non-functional interactions is severe. U...
We present a binding free energy function that consists of force field terms supplemented by solvati...
<p>(A) KGF-KITLG docked complex with spheres representing their binding interface. (B and C) DIMPLOT...
<p><sup>i</sup>N<sub>at</sub>: indicates the number of interfacing atoms</p><p><sup>i</sup>N<sub>res...
For a large number of protein it has now been stablishcd that their na-tives structures are thermody...
Absolute binding free energy calculations and free energy decompositions are presented for the prote...
Many cellular functions are based on the interaction and crosstalk of various signaling proteins. Am...
AbstractFormation of a stereospecific protein complex is favored by specific interactions between tw...
To clarify the interplay between the binding affinity and kinetics of protein-protein interactions, ...
SummaryAlthough protein-protein interactions are involved in nearly all cellular processes, general ...
AbstractWe report the computer generation of a high-density map of the thermodynamic properties of t...
Protein recognition is one of the most challenging and intriguing pro-blems in structural biology. D...
Protein-protein complexes orchestrate most cellular processes such as transcription, signal transduc...
<p>Interaction energy and interface Accessible Surface Area (ASA) in the minimized complexes emergin...
<p>Free energy estimated for noncovalent interactions involving active site residues Q39 and E451 an...
In the crowded cell, the competition between functional and non-functional interactions is severe. U...
We present a binding free energy function that consists of force field terms supplemented by solvati...
<p>(A) KGF-KITLG docked complex with spheres representing their binding interface. (B and C) DIMPLOT...
<p><sup>i</sup>N<sub>at</sub>: indicates the number of interfacing atoms</p><p><sup>i</sup>N<sub>res...
For a large number of protein it has now been stablishcd that their na-tives structures are thermody...
Absolute binding free energy calculations and free energy decompositions are presented for the prote...
Many cellular functions are based on the interaction and crosstalk of various signaling proteins. Am...
AbstractFormation of a stereospecific protein complex is favored by specific interactions between tw...
To clarify the interplay between the binding affinity and kinetics of protein-protein interactions, ...
SummaryAlthough protein-protein interactions are involved in nearly all cellular processes, general ...
AbstractWe report the computer generation of a high-density map of the thermodynamic properties of t...
Protein recognition is one of the most challenging and intriguing pro-blems in structural biology. D...
Protein-protein complexes orchestrate most cellular processes such as transcription, signal transduc...
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