Kevin C. Facemyer

Department:  Biochemistry and Molecular Biology
Academic Unit:  University of Nevada School of Medicine
Title:  Research Assistant Professor
Professional degrees (Degree, year, Institution): Ph.D. 1996, Washington State University

Contact Information

Mail Stop:  330
Phone:  327-2007
Fax:  784-1419
e-mail: facemyer@unr.edu

Research Area(s)

Biophysics, Biochemistry, Computational Chemistry:

Research Interests

Protein-protein interactions are one of the most fundamental molecular phenomena in biology. Protein-protein interfaces form the basis for the ability of proteins to perform work, provide structure, modulate cellular processes, and conduct metabolic processes. Experimental structural biologists have solved the structures of many proteins at various levels of resolution, but it is unlikely that the structures of all proteins complexes, oligomers, and macromolecular assemblies will be solved by experimental approaches. To rationally design therapeutics that effect diverse pathologies involving protein interactions, computational approaches are needed i) to further our understanding of the fundamental principles driving the formation of protein-protein interfaces and ii) to create robust methods for detecting and predicting interfaces.

Our work focuses on 2 aspects.  The first aspect is method development of an interface detection algorithm.  By using computational alanine scanning to score and detect native interfaces from docking runs we can indentify native interfaces where the crystal structures are known but the bounds states are not.  This capacity will enable computational detection of interacting proteins and facilitate rational drug design.  The second aspect is in using computational alanine scanning to analyze energy in protein interfaces, as well as intrafaces, and changes in energy during changes in protein conformation.  We combine these strategies and combine them with other computational techniques to understanding the changes in energy within protein structures such as actomyosin during the crossbridge cycle, smooth muscle myosin its downregulated state, paired calponin homology domains and their binding mechanisms to actin, unfolding of IG domains of titin and analyses of F1-ATPases. 

Other Lab Members

Emily Huang