B.D Nageswara Rao
Professor

Email Dr. Rao

Education

B.S., (Honors) Physics, Andhra University, Waltair (A.P.), India, 1955
M.S. Physics, Andhra University, Waltair (A. P.), India, 1956
Ph.D., Physics, Aligarh Muslim University, Aligarh (U. P.), India, 1961

Research

Our research program is in the general area of application of magnetic resonance techniques (NMR & EPR0 to the study of structure-function relationships in biological macromolecules. In particular, our recent efforts were directed at two types of proteins: 1. a group of ATP-utilizing enzymes; and 2. the proteins responsible for the bioluminescence of jellyfish.

Enzymes for which ATP is a substrate are ubiquitous since adenosine triphosphate (ATP) is utilized as a source of energy in a variety of biochemical pathways that occur inside the cell. Depending on the enzyme, either a phosphoryl, or a pyrophosphoryl or a nucleotidyl moiety is cleaved off from ATP and transferred to a second substrate. Regardless of where the cleavage occurs, a dicalent cation, usually Mg(II), is an obligatory component of these reactions. The group of enzymes we work with contains the three categories mentioned. NMR techniques are used to characterize the structure of the reaction complexes at the active-sites of these enzymes. A clear knowledge of such structures allows us to address specific questions such as the role of the cation in these reactions, as well as to provide information on the general question of the molecular basis of enzymatic action which is one of the central problems of biochemistry.

We have also been interested in magnetic resonance studies of the mechanism of the protein aequorin from jellyfish. In vitro, aequorin glows brilliantly blue upon binding Ca(II). Jellyfish glow green because the bioluminescent energy of aequorin is utilized by a second (green fluorescent) protein. Our work is aimed at the structure-function relationships of these interesting proteins.

Publications

Ray BD, Jarori GK, Yan H, Ragunathan V and Nageswara Rao BD (2005)
Conformation of Nucleotides Bound to Wild Type and Y78F Mutant Yeast Guanylate Kinase: Proton Two Dimensional Transferred NOESY Measurements.
Biochemistry 44, 13762-13770.

Ray BD, Jarori GK, and Nageswara Rao BD (2002)
Quantitation of Movement of the Phosphoryl Group During Catalytic Transfer in the Arginine Kinase Reaction: 31P Relaxation Measurements on Enzyme-Bound Equilibrium Mixtures.
J. Biomol. NMR 23, 13-21.

Ray BD, Khoroshev MI, Ue K, Morales MF, and Nageswara Rao BD (2002)
Changes in the 31P NMR Spectrum of Rabbit Muscle Myosin Subfragment-1·MgADP with Temperatures.
Arch. Biochemistry and Biophysics 402, 243-248.