title: Circular dichroism and its use in protein-folding studies.
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.
authors.affiliation: Central Laser Facility, Science and Technology Facilities Council, Research Complex at Harwell, Rutherford Appleton Laboratory, Didcot, UK. d.t.clarke@dl.ac.uk
authors.forename: David T
authors.initials: DT
authors.lastname: Clarke
mesh_terms: D002138:Calibration; D002942:Circular Dichroism / Q000379:methods*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins