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Position: Professor Emeritus
Voice: (410) 706-8102
E-mail:collins@umbi.umd.edu
Mailing info
MBC Faculty Directory
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Research Overview
Muscles have been studied from the perspectives of cellular and organismal biology and are also key topics in sports medicine and heart medicine (cardiology).
The proteins that allow muscles to contract and relax----and the elaborate cellular mechanisms that allow muscles to respond rapidly and reliably to electrical signals from the nervous system----have been studied in great detail, yet there is still much to be learned.
Several interacting proteins----especially proteins from the actin and myosin families----are responsible for muscle contraction. The microscopic structure of muscle tissues is now reasonably well understood.
Calcium acts as a secondary messenger in muscle tissue, and this is an active and fruitful area of study.
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Research Description
Research Specialties:
muscle regulatory proteins, protein structure and function, computer modeling, bioinformatics
I have been involved in structural studies on muscle proteins since 1969, starting as a postdoctoral fellow contributing to the original protein sequencing of actin and myosin. I did the original sequencing of troponin C and myosin light chains, showed that these proteins are homologous, and published accurate predictions of their three-dimensional structures. Subsequently, a total of more than twenty additional muscle and calcium-binding proteins from various sources were sequenced in my laboratory. These comparative studies helped to identify conserved regions with essential common functions and differences related to variations in their properties. More recently, I have applied the general protein and peptide chemistry techniques used in protein sequencing to other approaches such as chemical crosslinking and fluorescent probes. I have also shared my protein chemistry and sequencing expertise with many others in muscle and related fields over the years. My laboratory also expanded its experimental repertoire with new approaches for studying the structure and function of muscle proteins. We developed independent expertise in cloning, mutagenesis, DNA sequencing and expression of muscle proteins, purification of both natural and recombinant proteins, as well as various methods...
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Additional Information
UMBI Senate
Myoinformatics
CUSF
UMBI Professor since 1987
UMBI Senate Chair, 1993-1996 and 2002-2005
UMBI Senate member, 1992-1999 and 2002-2005
UMBI Senate web site administrator, 2002-2005
CUSF member since 1997
CUSF Chair, 2007-2008
CUSF Vice Chair, 2002-2003
CUSF Secretary, 2000-2002 and 2005-2007
CUSF At-Large Executive Committee member, 1998-2000
CUSF web site administrator since 2000
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Representative Publications
Emura, J., Ikenaka, T., Collins, J.H. and Schmid, K.: The constant and variable regions of the carboxyl terminal CNBr fragment of alpha-1-acid glycoprotein. J Biol. Chem. 246: 7821-7823, 1971.
Schmid, K., Brgi, W., Collins, J.H. and Nanno, S.: The disulfide bridges of alpha-1-acid glycoprotein. Biochemistry 13: 2694-2697, l974.
Schmid, K., Hediger, M.A., Brossmer, R., Collins, J.H., Haupt, H., Marti, T., Offner, G.D., Schaller, J., Takagaki, K., Walsh, M.T., Schwick, G., Rosen, F.S., and Remold-O'Donnell, E.: Amino acid sequence of human plasma galactoglycoprotein: Identity with the extracellular region of CD43 (sialophorin). Proc. Natl. Acad. Sci. USA 89: 663-667, 1992.
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