(Rams) Ayyalusamy Ramamoorthy, Ph.D.

Michigan Neuroscience Institute Affiliate
Robert W Parry Collegiate Professor Emeritus of Chemistry and Biophysics
Professor Emeritus of Macromolecular Science and Engineering

930 North University Avenue
Ann Arbor, Michigan 48109-1055

734-647-6572

Areas of Interest

My research group focuses on the investigation of the dynamic structures and function of membrane-associated proteins and protein-protein complexes, and understanding the role of membrane composition on protein folding, misfolding, and aging-related diseases. Two of the major research areas are: (1) Understanding folding/misfolding, aggregation, and toxicity of amyloid proteins (such as islet amyloid polypeptide (IAPP or amylin), amyloid-beta, alpha-synuclein) and the molecular processes governing liquid-liquid phase separation (LLPS). The many roles of cofactors (such as lipid membrane, metals, metabolites and small molecules) influencing protein aggregation are also investigated. (2) Development and applications of nanodiscs to study the structure and function of cytochrome enzymes and GPCRs. A variety of cutting-edge biophysical and biochemical approaches are used to address the biomedically important questions related to these topics.

Honors & Awards

  • Elected Fellow of the Royal Society of Chemistry (2018)
  • Distinguished Faculty Achievement Award, University of Michigan (2016)
  • Hans Fischer Senior Fellow, Technical University of Munich (2015)
  • Rackham Faculty Recognition Award (2012)
  • American Association for the Advancement of Science Fellow (2009)
  • Japan Society for the Promotion of Science Fellow (2009)
  • Willsmore Fellow, University of Melbourne, Australia (2009)

Published Articles or Reviews

  • Detergent-free isolation of CYP450-reductase's FMN-binding domain in E. coli lipid-nanodiscs using a charge-free polymer. Krishnarjuna B, Ravula T, Ramamoorthy A. Chem. Commun. (Camb). 2022 Mar 31. doi: 10.1039/d1cc07193a.
  • Saponins Form Nonionic Lipid Nanodiscs for Protein Structural Studies by Nuclear Magnetic Resonance Spectroscopy. McCalpin SD, Ravula T, Ramamoorthy A. J Phys Chem Lett. 2022 Feb 24;13(7):1705-1712
  • Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis. Nguyen et al. Chem Rev. 2021 Feb 24;121(4):2545-2647
  • Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes. Milardi D, Gazit E, Radford SE, Xu Y, Gallardo RU, Caflisch A, Westermark GT, Westermark P, Rosa C, Ramamoorthy A. Chem Rev. 2021 Feb 10;121(3):1845-1893.

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