The research goal of my laboratory is to understand the molecular motions and interactions of proteins involved in regulating contractile function of healthy cardiac and skeletal muscle, to determine the culprits of contractile dysfunction and remodeling in muscle disorders and cardiovascular disease, and then apply these insights to design novel therapies. We use biophysical approaches, such as time-resolved spectroscopy with site-directed probes to assess protein structural dynamics and mechanical measurements of isolated muscle fibers to assess contractile force and kinetics, in order to establish structure-function relationships inherent to the molecular, biochemical, and physiological mechanisms.
Brett Colson, PhD
Assistant Professor, Cellular and Molecular Medicine
Molecular Medicine Grad Program:
Colson, B. A., A. R. Thompson, M. L Espinoza-Fonseca, and D. D. Thomas, "Site-directed spectroscopy of cardiac myosin-binding protein C reveals effects of phosphorylation on protein structural dynamics.", Proc Natl Acad Sci U S A, vol. 113, issue 12, pp. 3233-8, 2016 Mar 22. PMCID: PMC4812748 PMID: 26908877
Colson, B. A., I. N. Rybakova, E. Prochniewicz, R. L. Moss, and D. D. Thomas, "Cardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner.", Proc Natl Acad Sci U S A, vol. 109, issue 50, pp. 20437-42, 2012 Dec 11. PMCID: PMC3528524 PMID: 23169656
Colson, B. A., J. R. Patel, P. P. Chen, T. Bekyarova, M. I. Abdalla, C. W. Tong, D. P. Fitzsimons, T. C. Irving, and R. L. Moss, "Myosin binding protein-C phosphorylation is the principal mediator of protein kinase A effects on thick filament structure in myocardium.", J Mol Cell Cardiol, vol. 53, issue 5, pp. 609-16, 2012 Nov. PMCID: PMC3472100 PMID: 22850286