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Donald A. Winkelmann, Ph.D.
Present Title:
Department of Pathology and Laboratory Medicine

Office Address:
Department of Pathology and Laboratory Medicine
Robert Wood Johnson Medical School
675 Hoes Lane, R218
Piscataway, New Jersey 08854



Dr. Winkelmann has worked in the areas of structural molecule biology and biophysics throughout his career. His scientific studies have focused on molecular motors and their tracks with a particular focus on myosin and actin. Early studies included the first crystallographic structure of a myosin motor domain, an accomplishment that has been seminal in guiding the research in the area of molecular motors for the last 25 years. Current research interests include the cellular regulation of the folding, assembly, and maintenance of striated muscle myosin, a process that is essential to adaptation of sarcomeres to physiological changes. His work on the expression of human b-cardiac myosin led to the determination of the structure of the b-cardiac myosin motor domain. The distribution and impact of disease associated mutations and drug-binding sites on the cardiac motor domain is a current focus of his research. Dr. Winkelmann has served as the director of the research EM laboratory for 25 years and is active in graduate and undergraduate teaching. He enjoys golf, travel, and plays electric and acoustic blues guitar for enjoyment.

Description of Research Expertise:
Protein structure and Function, Protein Folding and Molecular Motors
Since completion of my doctoral thesis on the structure and function of the small subunit of the bacterial ribosome 30 years ago, I have been working on structure-function studies related to the molecular motor myosin. This has included initiating the crystallography project that produce the first structure of a molecular motor. This accomplishment has been seminal in guiding the research in the area of molecular motors. My current research interests lie in the area of the cellular regulation of the folding, assembly and maintenance of striated muscle myosin; a process that is essential to adaptation of sarcomeres to physiological changes.

Undergraduate Education:
University of Wisconsin – Milwaukee
Department of Chemistry
Milwaukee, Wisconsin
B.S. 1973

Graduate Education:
University of Wisconsin
Department of Physiological Chemistry
Thesis: “Immunochemical Analysis of 30S Ribosome Structure”
Madison, Wisconsin
Ph.D. 1980

Postdoctoral Training:
Rosenstiel Center for Basic Research
Structural Biology Laboratory
Brandeis University
Waltham, MA
1980 - 1986

Selected Publications:

  • Srikalulam, R., Li Liu, and D.A. Winkelmann. 2008. Unc45b Forms a Cytosolic Complex with Hsp90 and Targets the Unfolded Myosin Motor Domain. PloS One vol. 3 issue 5: e2137.
  • Liu, L., R. Srikakulam and D.A. Winkelmann. 2008. Unc45 activates Hsp90 dependent folding of the myosin motor domain. J. Biol. Chem. 283(19):13185-93. doi:10.1074/ jbc.M800757200
  • Winkelmann, D.A. and R. Srikakulam. 2005. Chaperone Mediated Maturation of Striated Muscle Myosin. International Symposium of Muscular Contraction and Cell Movement, Colima, Mexico, Colima University Press.
  • Srikakulam, R. and D.A. Winkelmann. 2004. Chaperone-mediated Folding and Assembly of Myosin in Striated Muscle J. Cell Science. 117:641-652.
  • Wang, Q., C.L. Moncman and D.A. Winkelmann. 2003. Mutations in the Motor Domain Modulate Myosin Activity and Myofibril Organization. J. Cell Science 116:4227-4238.
  • Chow, D. R. Srikakulam, Y. Chen and D.A. Winkelmann. 2002. Folding of the Striated Muscle Myosin Motor Domain. J. Biol. Chem. 277:36799-36807.
  • Xiang, X., Gongshe Han, D.A. Winkelmann, Wenqi Zuo and N. Ronald Morris. 2000. Dynamics of cytoplasmic dynein in living cells and the effect of a mutation in dynactin complex actin-related protein Arp1. Current Biology 10:603-606.
  • Srikakulam, R. and D.A. Winkelmann. 1999. Myosin II Folding is Mediated by a Molecular Chaperonin. J. Biol. Chem. 274:27265-27273.