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Circular Dichroism and its use in Protein-Folding Studies

DOI: 10.1007/978-1-60327-223-0_5 DOI Help

Authors: David T. Clarke (Central Laser Facility)
Co-authored by industrial partner: No

Type: Book Chapter

State: Published (Approved)
Published: September 2011
Diamond Proposal Number(s): 7290 , 6131

Abstract: The way in which proteins fold into the complex 3 dimensional structures that are responsible for their function is a subject of great practical as well as fundamental significance because of the involvement of folding and misfolding in a number of serious human and animal diseases. Ultraviolet circular dichroism (CD) reports on the secondary and tertiary structure of proteins. Measurements can be made on proteins in the solution phase, and critically time-resolved measurements can be made with millisecond resolution. This combination of characteristics makes CD a useful tool for investigating protein folding, and indeed any process involving changes in protein structure. Experimental methods for a typical time-resolved CD experiment are described, and some common problems identified

Subject Areas: Biology and Bio-materials, Materials, Medicine

Instruments: B23-Circular Dichroism

Other Facilities: Yes, CD12