Character and evolution of protein-protein interfaces.
Protein-protein interactions create the macromolecular assemblies and sequential signaling pathways essential for cell function. Their number far exceeds the number of proteins themselves and their experimental characterization, while improving, remains relatively slow. For these reasons, novel computational methods have important roles to play in understanding the physical basis of protein interactions, and in constraining the molecular basis of their specificity. This paper discusses methods based on multiple sequence alignments of protein homologues and phylogenetic trees.
Res
Ivica
I
Department of Molecular and Human Genetics, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Lichtarge
Olivier
O
D001185:Artificial Intelligence; D001703:Biophysics / Q000379:methods*; D002468:Cell Physiological Phenomena; D019295:Computational Biology / Q000379:methods; D030562:Databases, Protein; D019143:Evolution, Molecular; D008968:Molecular Conformation; D011485:Protein Binding; D025941:Protein Interaction Mapping; D020836:Protein Structure, Quaternary; D011506:Proteins / Q000737:chemistry*; D015203:Reproducibility of Results; D016415:Sequence Alignment; D015398:Signal Transduction
D011506:Proteins