| Authorised form of name | Green; Norman Michael (1926 - 2019) |
| Dates | 1926 - 2019 |
| Nationality | British |
| Place of birth | Poldhu, Cornwall, England, United Kingdom |
| Date of birth | 06/04/1926 |
| Date of death | 12/08/2019 |
| Occupation | Biochemist |
| Research field | Proteins |
| Biochemistry |
| Activity | Education:
Dragon School, Oxford (1934-1939); Clifton College, Bristol (1939-1944); Magdalen College Oxford, MSc in Chemistry (1944-1948); University College Hospital, PhD in biochemistry (1948-1951)
Career:
Postdoctoral student, Department of Biochemistry, University of Washington, Seattle (1951-1953); Assistant Lecturer in Biochemistry, University of Sheffield (1953-1955); Department of Chemical Pathology, St Mary's Hospital Medical School (1955-1962); Visiting Scientist in the Laboratory of Organic Chemistry, National Institutes of Health, Bethesda (1962-1964); National Institute for Medical Research, London, Division of Biochemistry (1964-1985), Head of Laboratory of Protein Structure (1985-1992), affiliated to Laboratory of Mathematical Biology (1992- ). |
| Membership category | Fellow |
| Date of election | 19/03/1981 |
| Age at election | 54 |
| Relationships | Undergraduate tutors: L. E. Sutton FRS and F. E. King FRS.
Student contemporaries at Magdalen College Oxford: R. J. P. WIlliams FRS, P. C. Caldwell FRS, L. E. Orgel FRS and O. Smithies (Naubel Laureate 2007 molecular biology and genetics).
PhD supervisor: Professor C. Rimmington FRS
Worked with Professor H. Krebs FRS at University of Sheffield |
| OtherInfo | Norman Green made important and highly original contributions to the study of protein–protein interactions and interactions between proteins and biologically active small molecules. He established that the interaction between trypsin and several protein inhibitors was competitive with substrate rather than non-competitive as had been previously suggested. He also devised methods generally applicable to the measurement of kinetics of protein–protein interactions of very low dissociation constants. He showed that the hydroxylation of collagen proline was completed after its incorporation into the protein and before the collagen left the endoplasmic reticulum. This was followed by a decade of intensive research on the binding of biotin to avidin and the introduction of highly sensitive spectrophotometric techniques for the study of biotinyl enzymes. In particular, he made the important discovery that each of the four subunits of avidin bound its biotin independently of the occupancy of the other sites buried within the molecule, and that the quaternary structure of the protein was not essential for the formation of the binding site.
Dr Michael Green FRS died on 12 August 2019. |
| Source | Sources:
https://royalsociety.org/people/norman-green-11536/ |
| Code | NA4154 |
Archives associated with this Fellow
| RefNo | Title | Date |
| IM/GA/GRS/8587 | Green, Norman Michael | nd |
| EC/1981/17 | Green, Norman Michael: certificate of election to the Royal Society | 1975 |