David Phillips (1924-1999): A founding father of structural biology

Article Abstract:

David Phillips's structure determination of lysozyme in 1965 showed the power of protein crystallography to explain biological function in terms of physics and chemistry. Phillips was made professor of molecular biophysics at Oxford University in 1966, where, with his graduate students, he solved the structure of triose phosphate isomerase. He began a career in science policy and administration in the mid 1970s and he was chairman of the Advisory Board for the Research Councils (ABRC) between 1983 and 1993. He was appointed a life peer in 1994 and completed a manuscript on how the lysozyme molecule was actually solved only days before his death.

Biologists

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Fishing in Src-infested waters

Article Abstract:

One SH2 domain's macromolecular crystal structure consists of the Src proto-oncogene tyrosine kinase complexed with a peptide composed partly of phosphotyrosine. The determination of this SH2 domain's structure by Gabriel Waksman and colleagues should open the way to further research in cell biology. Moreover, the structure was found to be ideally modular, permitting this SH2 domain to be linked to protein sequences at any point without disrupting them.

Research, Cellular signal transduction, Protein tyrosine kinase, Protein-tyrosine kinase

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For medicinal purposes

Article Abstract:

The development of new techniques in pharmaceutical chemistry will help in the cheap and fast development of drugs. High-throughput screening of combinatorial libraries and structural techniques will replace the natural products based medicinal chemistry. The development of a specific drug will be based on genomics or cell biology research. Natural products, oligonucleotides, combinatorial organic compounds and molecules will help in this search.

Drugs, Reports, Design and construction, Pharmaceutical chemistry

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