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TERRY L. DOWD 

Associate Professor

Department of Chemistry

Brooklyn College

2900 Bedford Ave.

Brooklyn, N.Y. 11210

 

TELEPHONE 

  • Office 1-718-951-5000 (2847)

  • Lab     1-718-951-5000 (4761)

 

EMAIL ADDRESS

TDowd@brooklyn.cuny.edu

 

 

EDUCATION

 

Syracuse University                              Ph.D.                  (1987)  Physical Chemistry

 

Southern Connecticut State College     B.S.                    (1979)  Chemistry

 

Postdoctoral Fellow,     Department of Physiology and Biophysics

                                      Albert Einstein College of Medicine  (1986-1987)

 

CAREER

 

2005 – Present           Associate Professor, Department of Chemistry

                                   Brooklyn College, City University of New York

 

2005- Present             Visiting Assistant Professor, Department of Neuroscience

                                    Albert Einstein College of Medicine, Bronx, New York

 

1996 – 2004               Assistant Professor, Division of Environmental Sciences,

                                   Department of Pediatrics, Montefiore Medical Center,                                                                     

                                   Albert Einstein College of Medicine, Bronx, New York

 

1992 - 1996                 Instructor, Department of Physiology and Biophysics,

                                    Albert Einstein College of Medicine

 

1987 - 1992                 Research Associate, Department of Physiology and Biophysics, 

                                    Albert Einstein College of Medicine

 

1986 - 1987                 Postdoctoral Fellow, Department of Physiology and Biophysics

                                    Albert Einstein College of Medicine.

 

 

RESEARCH INTERESTS

 

      My research has produced 19 papers and 1 book chapter. I have always used physical techniques to study biological or medically related questions. I have used NMR spectroscopy to investigate alterations in intracellular cations in various diseases and conditions. I have investigated alterations in intracellular cations in hypertensive rat kidneys as well as in kidneys from hyperglycemic rat models. Since bone is the major reservoir of body lead I was interested in the effect of lead toxicity on intracellular cations and bioenergetic rates in perfused bone cells. My interests have evolved into the area of protein structure and functional studies and alterations in structure due to lead toxicity and amino acid mutations. Information regarding molecular function can be obtained by solving the high resolution structures of a protein or peptides. 

 

CURRENT RESEARCH PROJECTS 

    My research is focused on structural and functional studies of the bone protein osteocalcin. Osteocalcin is a small protein of 49 amino acid residues and is one of the most abundant noncollagenous proteins found in bone, dentin and cementum. In-vivo studies with the osteocalcin knock-out mouse suggest osteocalcin may function to limit bone formation. The effect of osteocalcin on crystal size and “perfection” suggest a role in bone remodeling. I am particularly interested in how the effects of metal ions, toxic (Pb2+) and essential (Mg2+) alter the structure and mineral binding properties of osteocalcin and how these effects are manifested in detailed bone mineral properties and bone biomechanical properties in a living animal.  I use techniques such as ELISA protein assays, Fourier Transform Infrared Microscopy and Imaging, MicroCt imaging and Atomic Absorption spectroscopy to conduct this research.

 

    I am also interested in structure function relationships in N-terminal peptides of the gap junction protein Connexin. Gap junctions allow the passage of small molecules and second messengers between cells. They can be modulated by voltage dependent gating. There is evidence that the N-terminus of some Connexins may act as a voltage sensor and is located within the channel pore. We are investigating the structure of a functional Connexin channel by structural studies of Connexin N-terminal peptides (both mutants and wildtype) using high resolution NMR spectroscopy.