title: Biophysical and computational methods to analyze amino acid interaction networks in proteins.
abstract: Globular proteins are held together by interacting networks of amino acid residues. A number of different structural and computational methods have been developed to interrogate these amino acid networks. In this review, we describe some of these methods, including analyses of X-ray crystallographic data and structures, computer simulations, NMR data, and covariation among protein sequences, and indicate the critical insights that such methods provide into protein function. This information can be leveraged towards the design of new allosteric drugs, and the engineering of new protein function and protein regulation strategies.
authors.affiliation: Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA.
authors.forename: Kathleen F
authors.initials: KF
authors.lastname: O'Rourke
authors.affiliation: Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA.
authors.forename: Scott D
authors.initials: SD
authors.lastname: Gorman
authors.affiliation: Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA.
authors.forename: David D
authors.initials: DD
authors.lastname: Boehr
keywords: Allostery; Amino acid interaction network; CONTACT; Coevolution; Elastic network; Graph theory; Molecular dynamics; NMR; Statistical coupling analysis