Biochemistry & Pharmacology: Open Access
Open Access
ISSN: 2167-0501
ISSN: 2167-0501
John Cavanagh
Department of Molecular and Structural Biochemistry, North Carolina State University, USA
Dr. Cavanagh is the William Neal Reynolds Distinguished Professor of Biochemistry at NC State University. He is an expert in structural biology and how bacteria are able to protect themselves. He received his Ph.D. in Chemistry/NMR spectroscopy from the University of Cambridge in 1988. He has held positions as a Senior Research Associate at The Scripps Research Institute, Director of NMR Structural Biology at the Wadsworth Center, Assoc. Prof. of Biomedical Sciences (SUNY) and Prof. of Chemistry (Purdue). Since 2000 he has been in the Department of Molecular & Structural Biochemistry at NC State. He has served on numerous NIH and NSF grant review panels. He is author or co-author of over 100 research publications and co-author of the successful textbook "Protein NMR Spectroscopy." He has been awarded the Foulerton Gift & Binmore Kenner Fellowship of the Royal Society (1990), The Fullsome Award (1996) and NC State University Alumni Associations Outstanding Research Award (2005).
The Cavanagh lab is generally interested in how the specific structure and inherent flexibility of proteins helps them carry out their biological roles. For a few years and with some success, his main focus has been on proteins involved in bacterial response/protection and the development of infectious disease. These are proteins that enable bacteria survive in difficult circumstances/environments and help them reach their pathogenic potential. The main types of proteins we study are response regulator proteins and transition state regulator proteins. Please see our 'Research' section for a little more information. He is also very interested in neurodegenerative processes such as Alzheimer's disease. He have been studying the role of the calcium-binding protein calbindin D28K in suppressing the onset of Alzheimer's. Calbindin D28K appears to regulate both the amyloid and neurofibrillary tangle pathologies that define the disease.