Surface plasmon resonance facility for biochemistry and pharmacology

Lead Research Organisation: University of Cambridge
Department Name: Biochemistry


Now that the DNA sequence of the human and other genomes has been determined it is necessary to understand how the individual gene products encoded interact with each to generate the complexity characteristic of biological systems. Surface plasmon resonance is a technique that allows interactions between biological molecules such as proteins and nucleic acids to be assessed quantitatively and allows insights into how these interactions regulate biological processes. The BIACORE T100 instrument will be a powerful tool for this cutting edge research and will support not only the seven applicants but other groups in the Schools of Biological and Physical Sciences.

Technical Summary

Compared to its predecessors, the BIACORE T100 has considerably enhanced sensitivity and the ability to detect interactions with small molecules down to Mr 200. The machine also has temperature control and can process up to 384 samples automatically in multi-well format. It also allows thermodynamic parameters to be measured, sample recovery and measurements in up to four different buffer systems simultaneously. Thus this instrument will play a central role in the high-quality projects involving cellular regulation described in the application and is likely also to be used by others in the Schools of Biological and Physical Sciences not included in the application. The projects that will be enhanced and supported by this equipment are: (1) Signal transduction by the pattern recognition receptors of the innate immune system (2) Detecting the early responses of tumours to therapy (3) The interaction of platelet receptors and other molecules with collagen (4) Protein-protein interactions in chromatin mediated silencing (5) Structure of macromolecular assemblies: the degradosome (6) Role of PfEMP1 protein in malaria pathogenicity (7) Ligand binding to the the ion channel TRPV1 (8) The structural basis for docking in modular mega-synthases


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