Vincent A. Barnett, PhD

Assistant Professor, Department of Integrative Biology and Physiology (IBP)

Vincent A. Barnett

Contact Info

Office Phone 612-624-8135

Fax 612-625-5149

Office Address:
3-136 Jackson H
321 Church Street S.E.
Minneapolis, MN 55455

Mailing Address:
6-125 Jackson Hall
321 Church Street S.E.
Minneapolis, MN 55455

PhD, University of Minnesota (Biochemistry), 1987

MS, University of Minnesota (Biochemistry), 1984

BS, Oregon State University (Biochemistry and Biophysics), 1979


Research Summary/Interests

My work focuses on the physiology and biophysics of skeletal muscle. The work focuses primarily on probing the interactions of actin and myosin and the role of the passive resistance provided by titin protein filaments. I am interested in the relationship between macromolecular structures and their physiological functions. I the intricate organization and interaction of macromolecules in skeletal muscles and in the eye provide model systems for the study of the coupling of form and function. It is our hope that this combination of mechanical and biochemical data will help us to relate better molecular level information to the physiological responses to biological tissues.


PUBMED List of Publications

  • Barnett V.A. (2005) Cardiac Myocytes. In Handbook of Cardiac Anatomy, physiology, and Devices, paul A. Iaizzo editor. Humana press pp. 113-121.
  • Barnett, V.A. (2001) Cross-bridge Cooperativity during Isometric Contraction and Unloaded Shortening of Skeletal Muscle. J. Mus. Res. Cell Motil. 22:415-423.
  • Xie, L., Li, W.X., Barnett, V.A. & Schoenberg, M. (1997). Graphical Evaluation of Alkylation of Myosin’s SH1 and SH2: The N-phenylmaleimide reaction. Biophys. J. 72:858-865.
  • Ehrlich, A., Barnett, V. A., Chen, H. & Schoenberg M. (1995). The Site and Stoichiometry of the N-phenylmaleimide Reaction With Myosin When Weakly- binding Crossbridges are Formed in Skinned Rabbit psoas Fibers. Biochem. Biophys. Acta 1232: 13-20.
  • Ostap, E. M., Barnett V. A. & Thomas, D. D. (1995). Resolution of Three Structural States of Spin-labeled Myosin in Contracting Muscle. Biophys. J. 69:177-188.