UNIT 28.3 Circular Dichroism in Protein Folding Studies

  1. David T. Clarke

Published Online: 1 NOV 2012

DOI: 10.1002/0471140864.ps2803s70

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Clarke, D. T. 2012. Circular Dichroism in Protein Folding Studies. Current Protocols in Protein Science. 70:28.3:28.3.1–28.3.17.

Author Information

  1. Central Laser Facility, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Didcot, Oxfordshire, United Kingdom

Publication History

  1. Published Online: 1 NOV 2012
  2. Published Print: NOV 2012


Protein folding is a biological process of both fundamental significance and practical importance, and protein misfolding is implicated in a number of serious diseases of both humans and animals. The study of protein folding requires a technique that is able to monitor changes in protein structure in solution, with millisecond time resolution. Ultraviolet circular dichroism (CD) is such a technique, providing information on both secondary and tertiary protein structure. This unit describes the procedures for performing CD experiments for the study of protein folding, and identifies commonly encountered problems and their solutions. Curr. Protoc. Protein Sci. 70:28.3.1-28.3.17. © 2012 by John Wiley & Sons, Inc.


  • protein folding;
  • circular dichroism;
  • stopped-flow;
  • protein structure