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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 binding dynamics:

Recent advances on our understanding of protein binding has shown that the onset of this process is not the fully desolvated interface, dominated by van der Waals interactions, but instead a smoother landscape governed by the the long-range (10 A) electrostatics and intermediate-range (5 A) solvation forces between molecules. These forces, which provide the initial attraction between ligands and their receptors, were also found consistent with a relatively narrow docking pathway to the final bound conformation. On the other hand, it is well known that surface complementarity, led by short-range vdW forces, play a crucial role on the stability and specificity of the high affinity complex. These properties indicate that the intrinsic dynamic nature of protein binding leads to distinct kinetic regimes where different driving forces with diverse length scales governed the binding process at different times. [1]|[2]|[3]

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


Public Servers

Protein interactions:
NEW Validation CAPRI3-5.PDF

Homology modeling:
CAFASP3 benchmark
NEW Modeling side chains.PDF

Protein-protein interactions:
NEW FastContact

Splitting structural domain:


NEW FastContact PDF

Public Databases

Docking decoys