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Structural studies on Fab/hCG complexes: protein- protein recognition and structural mapping of epitopes
Reference
B09687
Principal Investigator / Supervisor
Professor Neil William Isaacs
Co-Investigators /
Co-Supervisors
Institution
University of Glasgow
Department
School of Chemistry
Funding type
Research
Value (£)
130,161
Status
Completed
Type
Research Grant
Start date
01/10/1998
End date
01/10/2001
Duration
36 months
Abstract
Crystals have been grown for a number of fab/hCG complexes, and conditions have been established for the formation of ternary fab/hCG/Fab complexes. The aim of the study is to determine the crystal structures of a number of different Fab/hCG complexes. Fab/hCG/Fab type complexes and isolated Fab molecules. From this study we shall determine the complete epitope surface of the hormone and establish those structural factors important in determining the strength and specificity of protein-protein interactions. Structures of ternary Fab/hCG/Fab complexes will show factors important in synergistic binding effects observed with second antibody binding. The work will bear directly on hormone - receptor studies. it is expected that a better, more accurate and complete structure of hCG will be obtained from structures of Fab/hCG complexes.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
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