معرفی
Dr. Ross Dalbey is a Full Professor in the Department of Chemistry and Biochemistry at The Ohio State University, affiliated with the College of Arts and Sciences. He holds a B.S. in Chemistry from the University of Washington (1978) and a Ph.D. in Biochemistry from Washington State University (1983). Postdoctoral training included work with Prof. William Wickner at UCLA. His research focuses on membrane protein assembly and proteases, particularly the YidC protein's role in membrane insertion and folding. Key areas include biophysical mechanisms of protein insertion, signal peptidase function, and mitochondrial membrane systems. He has held NIH and AAAS fellowships, and his lab has been funded by NIH and NSF for over three decades. His students hold academic and industry positions at institutions like NIH, MIT, and pharmaceutical companies such as Eli Lilly.
- Education:
- B.S., Chemistry, University of Washington, 1978
- Ph.D., Biochemistry, Washington State University, 1983
- Awards:
- American Cancer Society Junior Faculty Award (1989–1992)
- Elected Fellow of the American Association for the Advancement of Science (AAAS)
- Professional Memberships:
- American Chemical Society
- Federation of American Societies for Experimental Biology
- American Society of Microbiology
- Sigma Xi
- Phi Kappa Phi
His lab investigates how proteins are inserted into membranes and folded, with emphasis on the YidC/Oxa1 family of insertases. Recent work explores YidC's substrate specificity, dimeric structure, and interactions with the Sec translocon. Studies on proteases like signal peptidase reveal their roles in membrane-associated peptide cleavage. Collaborations include structural biology with Prof. Horst Vogel in Switzerland and functional analyses with Prof. White at Ohio State.
Research highlights include defining YidC's role in multispan membrane protein integration and uncovering evolutionary conservation across bacterial, archaeal, and eukaryotic systems. The lab's findings contribute to understanding mitochondrial protein insertion pathways and drug design targeting membrane-associated enzymes.
