Paul D. Boyer

1997 Nobel Prize Winner
Citation
(Shared with John E. Walker) for their elucidation of the enzymatic mechanism underlying the synthesis of adenosine triphosphate (ATP)
Member, National Academy of Sciences
Election Year: 1970
Research/Expertise: enzyme structure and mechanism, rotational catalysis by the ATP synthase

 

 
Richard E. Dickerson

Member,
National Academy of Sciences
Election Year: 1985
NAS Section: Biophysics and Computational Biology
Citation

Dickerson is recognized for his pioneering studies on x-ray analysis of proteins, his cogent structural and evolutionary analyses of cytochromes c, his elegant treatises on protein structure and, more recently, for detailed structural analyses of crystalline double-helical DNA and its complexes with antitumor drugs.
 

 
 


David S. Eisenberg

Member,
National Academy of Sciences
Election Year: 1989
NAS Section: Biophysics and Computational Biology
Citation

Eisenberg's concepts of hydrophobic moment, atomic solvation parameters, and profiles, derived from his crystal structure of melittin, have changed our understanding of protein chain folding, domain assembly, and relatedness of amino acid sequences. His massive glutamine synthetase and RuBisCO structures have revealed enzymatic active sites shared between subunits and suggested means for catalytic control.

 

 


Wayne L. Hubbell

Member,
National Academy of Sciences
Election Year: 2005
NAS Section: Biophysics and Computational Biology
Citation

Hubbell has made fundamental contributions to our understanding of biological membranes and membrane proteins by development and application of site-directed spin labeling. His work has led to seminal discoveries including the membrane fluidity gradient and the rigid body motion of alpha-helices as the "central dogma" of receptor activation.

 




 


Joan S. Valentine

Member, National Academy of Sciences
Election Year: 2005
NAS Section: Chemistry
Citation

Valentine is a leading figure working at the interface of inorganic chemistry and biology. She has pioneered the chemistry of superoxide anion and its significance to life processes, including the mechanism responsible for familial amyotrophic lateral sclerosis ("Lou Gehrig's Disease"). Her work continues to influence the course of biomedical research.

 
Home

Webmaster - Penny Jennings