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Carlos J. Camacho
Structural Bioinformatics Lab
Department of Computational Biology
University of Pittsburgh

Research Projects

Protein-protein interactions

Protein binding dynamics

Protein docking

Protein-DNA interactions

Homology modeling
CASP5 results

Genomics and molecular evolution

Thermodynamic & dynamics of protein folding


Protein-Protein interactions:

Using explicit water molecular dynamics simulations and free energy estimates we try to understand the mechanisms of protein recognition. Our efforts have recently unveiled a new view on this subject, emphasizing the role of desolvation as a dominant force in recognition. We have also found that nanoscale receptor-ligand interactions stemming from electrostatic and solvation effects tunes the association time scales over a range spanning as much as 5 orders of magnitude in complexes where long electrostatics provide the specificty for recognition. Desolvation mediated complexes only span 3 order magnitude. Simulations have explicitly revealed that recognition arises from an optimized molecular key already encoded in the protein's primary structure. Similarly, well defined non-covalent, and non-specific, bonds are responsible for locking the encounter complex in place.

See Anchor residues in protein-protein interactions, PNAS 2004

Publications | Curriculum Vitae | Group/Collaborators | Useful Links

Carlos J. Camacho
Associate Professor
Department of Computational Biology
Department of Molecular Genetics and Biochemistry
University of Pittsburgh
W1041 Biomedical Science Tower
200 Lothrop St.
Pittsburgh, PA 15261
Office: (412) 648-7776
Fax: (412) 648-3163

Anchor Residues in Protein Recognition, PNAS 2004 SmoothDock, PNAS 2001