| RefNo | EC/1990/18 |
| Level | Item |
| Title | Johnson, Louise Napier: certificate of election to the Royal Society |
| Date | 1987 |
| Description | Citation typed |
| Citation | Distinguished for her contributions to protein crystallography and to the understanding of enzyme structure and activity. As a graduate student, she was the first to study complexes between an enzyme (lysozyme) and competitive inhibitors in detail crystallographically. Her results provided the basis for the first model of an enzyme-substrate complex and the first formulation of a stereochemical mechanism of enzyme catalysis. Subsequently she solved the structure of the very-large enzyme glycogen phosphorylase and determined the binding sires of its substrate and allosteric effectors. Her results have provided the basis for stereochemical interpretations of the control of the enzyme's activity by allosteric effectors and by reversible phosphorylation. She and her colleagues were instrumental in developing techniques for data collection from protein crystals by means of synchrotron radiation: by exploiting the bright X-ray beam at the syncrotron source at Daresbury (which enabled data-collection times to be reduced from 1 week to 0.5 hours), they have for the first time monitored the conversion of an enxyme-substrate to an enzyme-product complex in crystals in structural detail. Recent work with Laue diffraction methods has allowed a further reduction in data-collection times to less than 2 seconds and a finer time resolution of events in the crystal. |
| AccessStatus | Closed |
Fellows associated with this archive
| Code | PersonName | Dates |
| NA4932 | Johnson; Dame; Louise Napier (1940 - 2012) | 1940 - 2012 |