Donald L. D. Caspar

Florida State University


Election Year: 1994
Primary Section: 29, Biophysics and Computational Biology
Secondary Section: 22, Cellular and Developmental Biology
Membership Type: Member

Research Interests

How are virus particles assembled and how do protein molecules move to build complicated structures, send and receive signals, and catalyze vital processes? These are the broad questions on which my research in structural biology has been focused. The quasi-equivalence theory of icosahedral virus constructions that I formulated with Aaron Klug in 1962 was based on the recognition that the structural proteins must be plastically adaptable molecules that can self-assemble by linking together in different ways within a highly ordered structure. Studies on macromolecular assemblies over the past three decades, including critical x-ray diffraction, electron microscopy, and physiochemical results from my laboratory, have established the versatility of molecular plasticity in the construction and action of complex biological structures. Conformational switching, involved in regulated biomolecular functions, is dependent on the restrained mobility of the surrounding water. Methods have been developed in my laboratory to map the average disordered solvent structure in well-ordered protein crystals from x-ray diffraction data, and to characterize the coupling of the macromolecular atomic movements from the diffuse x-ray scattering. These and related biophysical methods are being applied to study the dynamics of structural proteins, hormones, and repressors.

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