CWRU Links
{{dept_full_name}}
Ayyalusamy ("Rams") Ramamoorthy, PhD
Robert W. Parry Collegiate Professor of Chemistry and Biophysics
University of Michigan
PhD, Indian Institute of Technology (Kanpur, India)
MSc, Chemistry, Madurai Kamaraj University (India)
BSc, Chemistry, Madurai Kamaraj University

Mailing Address:
Ann Arbor , MI
ramamoor@umich.edu

Research Interests

Physical Chemistry; Chemical Biology; Biomacromolecular Chemistry; Macromolecular Nanochemistry; Analytical Chemistry; Materials Chemistry; Imaging & Spectroscopy; Theory & Computation; Pharmaceutical Chemistry

Membrane proteins act as enzymes, regulate transport processes, and play a central role in intercellular communication. In order to understand the diverse functions of membrane proteins and to engineer these functions for biomedical or biotechnological purposes, it is necessary to determine their high-resolution structure and to describe their dynamics. Structure determination of membrane proteins is one of the most important and challenging aspects of science at the present time. Solid-state NMR spectroscopy is an ideal technique for immobile and non-crystalline proteins that are difficult to study by X-ray crystallography or by solution NMR.

The development of solid-state NMR methods and their applications to determine the structure and describe the dynamics of membrane proteins are the main goals of the research program. Biology of the research program involves the preparation of peptides and proteins associated with membranes through synthetic or molecular biological methods. All aspects of sample preparation are optimized including the incorporation of specific and selective isotopic labels, isolation, purification, and final preparation of NMR samples. Antimicrobial peptides, toxins, cytochrome b5, myelin basic protein, and amyloid peptides are some of the systems currently under investigation by this group. Solid-state NMR experiments on membrane proteins incorporated in oriented and unoriented phospholipid bilayers and solution NMR experiments on membrane proteins in detergent micelles or lipid bicelles are performed to determine the structure of membrane proteins.

Solid-state NMR spectroscopy is one of the premier methods for studying the structure and dynamics of molecules in solids. Dr. Ramamoorthy's research program orchestrates the theoretical design, experimental demonstration, and application of new and cutting edge solid-state NMR spectroscopic methods to study the structure and properties of molecules in single crystalline, liquid crystalline, polycrystalline, and amorphous phases. The design of solid-state NMR methods is composed of a variety of sophisticated techniques including specifically constructed multiple radio-frequency pulses, magic-angle spinning, multiple resonance schemes, sensitivity enhancement procedures, selective observation or hybridization of them. This basic research on spin physics encompasses theoretical and experimental aspects of spin engineering, computer simulations, and instrumentation.

Sources:  https://lsa.umich.edu/chem/people/faculty/ramamoor.html; http://rams.biop.lsa.umich.edu/research 

Related Links