Department of Biochemistry & Biophysics (B&B)
Graduate Student Perspectives

When I first visited the University of Rochester I was impressed with the sense of community within the department of Biochemistry and Biophysics. There were many venues for encouraging interactions and collaboration between students and faculty outside their own research groups. more ...
Joseph Liberman
The Department of Biochemistry & Biophysics (B&B) strives to understand the molecular mechanisms of important biological processes, thereby providing insight into how disruption of these mechanisms causes disease. Departmental research is generously supported by the National Institutes of Health (NIH). NIH instrument funds have contributed to our recent two million dollar investment in cutting edge structural biology, biophysical and mass spectrometry-based equipment. Furthermore, income generated from intellectual property derived from departmental research discoveries continues to be reinvested back into the department, and used to stimulate the genesis of private biotechnology companies.
In addition to supporting our research, the NIH has recognized our excellence in the Biochemistry & Molecular Biology (BMB) and Biophysics, Structural & Computational Biology (BSCB) Ph.D. programs by awarding the university a highly competitive interdepartmental T32 graduate training grant. Our commitment to graduate education is apparent from the positions acquired by our previous students and fellows, who are professors at major research universities and leaders in corporate research. Our continued focus on pioneering research and quality education ensures our position as a premier Biochemistry & Biophysics department.
Jeffrey J. Hayes , Ph.D.
Chair, Department of Biochemistry & Biophysics
Featured Research Images
Protein synthesis: the ribosome crystal structure showing tRNAs bound to the A, P and E sites. more info...
Latest News
Recent Publications
- (2012 May 18). Identifying Functionally Important Conformational Changes in Proteins: Activation of the Yeast α-factor Receptor Ste2p. J Mol Biol. 418, 367-78.
- (2012 May 14). The human biliverdin reductase-based peptide fragments and biliverdin regulate protein kinase Cδ activity: the peptides are inhibitors or substrate for the PKC. J Biol Chem. In press.
- (2012 May 07). Biochemical analyses indicate that binding and cleavage specificities define the ordered processing of human Okazaki fragments by Dna2 and FEN1. Nucleic Acids Res. In press.






