1994 - Fellow of John Simon Guggenheim Memorial Foundation
1994 - Member of the National Academy of Sciences
1972 - Fellow of the American Academy of Arts and Sciences
His main research concerns Particle, Tobacco mosaic virus, Crystallography, Molecular physics and Biophysics. His study in Tobacco mosaic virus is interdisciplinary in nature, drawing from both RNA, Nucleic acid and Nanotechnology. His biological study spans a wide range of topics, including Protein structure, Protein subunit, Electron density and Electron microscope.
Donald L. D. Caspar combines subjects such as Tropomyosin and Microscopy with his study of Electron microscope. The concepts of his Molecular physics study are interwoven with issues in Scattering, Diffraction and Protein crystallization. In Biophysics, Donald L. D. Caspar works on issues like Recombinant DNA, which are connected to Capsid, Saccharomyces cerevisiae, Scanning transmission electron microscopy and Fibril.
Donald L. D. Caspar mainly focuses on Crystallography, Diffraction, Molecular physics, X-ray crystallography and Biophysics. His work carried out in the field of Crystallography brings together such families of science as Protein structure, Capsid and Electron microscope. His study focuses on the intersection of Diffraction and fields such as Electron density with connections in the field of Bilayer.
Within one scientific family, Donald L. D. Caspar focuses on topics pertaining to Amplitude under Molecular physics, and may sometimes address concerns connected to Protein crystallization. His Biophysics study incorporates themes from Membrane and Biochemistry. His work in Helix addresses issues such as Protein subunit, which are connected to fields such as RNA.
The scientist’s investigation covers issues in Crystallography, Biophysics, Molecular biology, Mutant and Peptide. His Crystallography research is multidisciplinary, incorporating elements of X-ray crystallography, Bilayer and Protein folding. In his study, which falls under the umbrella issue of X-ray crystallography, Analytical chemistry is strongly linked to Scattering.
The Analytical chemistry study combines topics in areas such as Amplitude and Diffraction. His Biophysics research is multidisciplinary, incorporating perspectives in Electron diffraction, Strain, Yeast and Microscopy. His Peptide research integrates issues from Scanning transmission electron microscopy and Beta.
Donald L. D. Caspar mostly deals with Crystallography, Biophysics, Protein folding, Phytoreovirus and Microscopy. His Crystallography research incorporates elements of Electron microscope, Electron diffraction and Beta sheet. His Biophysics research incorporates themes from Scanning transmission electron microscopy, Strain, Biochemistry and Recombinant DNA.
His Protein folding study integrates concerns from other disciplines, such as Protein tertiary structure, Tryptophan, Mutant and Leucine, Isoleucine. He has included themes like Monolayer, Icosahedral symmetry, Cryo-electron microscopy and Capsid in his Phytoreovirus study.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Physical Principles in the Construction of Regular Viruses
D. L. D. Caspar;A. Klug.
Cold Spring Harbor Symposia on Quantitative Biology (1962)
Assembly and Stability of the Tobacco Mosaic Virus Particle
Advances in Protein Chemistry (1964)
Gap junction structures. I. Correlated electron microscopy and x-ray diffraction
D L Caspar;D A Goodenough;L Makowski;W C Phillips.
Journal of Cell Biology (1977)
Self-assembly of purified polyomavirus capsid protein VP1
Dinakar M. Salunke;Donald L.D. Caspar;Robert L. Garcea.
Polyoma virus capsid structure at 22.5 Å resolution
I. Rayment;T. S. Baker;D. L. D. Caspar;W. T. Murakami.
The structure of small viruses.
A. Klug;D.L.D. Caspar.
Advances in Virus Research (1961)
Tropomyosin: crystal structure, polymorphism and molecular interactions.
D.L.D. Caspar;Carolyn Cohen;William Longley.
Journal of Molecular Biology (1969)
Myelin membrane structure at 10 A resolution.
D. L. D. Caspar;Daniel A. Kirschner.
Movement and self-control in protein assemblies. Quasi-equivalence revisited.
Biophysical Journal (1980)
Gap junction structures. V. Structural chemistry inferred from X-ray diffraction measurements on sucrose accessibility and trypsin susceptibility.
Lee Makowski;D.L.D. Caspar;W.C. Phillips;D.A. Goodenough.
Journal of Molecular Biology (1984)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below: