Circular Dichroism (CD) | Peptide-Protein Materials Center (PPMC)

Circular dichroism (CD) spectroscopy is an analytical technique used to analyze chirality in molecules through their optical activity. CD measures the difference in absorption of left- and right-handed circularly polarized light. This technique is often used to determine secondary structures of peptides and proteins. Included below are a variety of scientific resources that detail circular dichroism and methods for obtaining the CD spectra of peptide and protein samples, as well as ways different properties can be deduced through CD experiments. For those that would like to learn more, stay tuned for a training video for our Jasco J-1500 Circular Dichroism Spectrophotometer that will be another great resource worth checking out!

General Background

This section provides background information on circular dichroism (CD) spectroscopy and its use in characterizing peptides and proteins. The most general and recommended articles are listed at the top of this section.

Tools and Methods for Circular Dichroism Spectroscopy of Proteins: A Tutorial Review

A. J. Miles, Robert W. Janes, B. A. Wallace

Chem. Soc. Rev., 50 8400-8413 (2021).

DOI: 10.1039/D0CS00558D

Circular Dichroism and Optical Rotatory Dispersion of Proteins and Polypeptides

Alice J. Adler, Norma J. Greenfield, Gerald D. Fasman

Methods Enzymol., 27 675-735 (1973).

DOI: 10.1016/S0076-6879(73)27030-1

Circular Dichroism of Biological Macromolecules

Sherman Beychok

Science, 154 1288-1299 (1966).

DOI: 10.1126/science.154.3754.1288

How to Study Proteins by Circular Dichroism

Sharon M. Kelly, Thomas J. Jess, Nicholas C. Price

Biochim. Biophys. Acta, Proteins Proteomics, 1751 119-139 (2005).

DOI: 10.1016/j.bbapap.2005.06.005

Using Circular Dichroism Spectra to Estimate Protein Secondary Structure

Norma J. Greenfield

Nat. Protoc., 1 2876-2890 (2006).

DOI: nprot.2006.202

Analysis of the Kinetics of Folding of Proteins and Peptides Using Circular Dichroism

Norma J. Greenfield

Nat. Protoc., 1 2891-2899 (2006).

DOI: nprot.2006.244

Using Circular Dichroism Collected as a Function of Temperature to Determine the Thermodynamics of Protein Unfolding and Binding Interactions

Norma J. Greenfield

Nat. Protoc., 1 2527-2535 (2006).

DOI: nprot.2006.204

Determination of the Folding of Proteins as a Function of Denaturants, Osmolytes, or Ligands Using Circular Dichroism

Norma J. Greenfield

Nat. Protoc., 1 2733-2741 (2006).

DOI: nprot.2006.229

Applications of Circular Dichroism in Protein and Peptide Analysis

Norma J. Greenfield

TrAC, Trends Anal. Chem., 18 236-244 (1999).

DOI: 10.1016/S0165-9936(98)00112-5

Circular Dichroism

Robert W. Woody

Methods Enzymol., 246 34-71 (1995).

DOI: 10.1016/0076-6879(95)46006-3

Characterizing Bundlemer Coiled Coils

For those interested in characterizing the structure of coiled-coil bundlemers utilizing circular dichroism (CD) spectroscopy, the following articles provide some examples of prior characterization of these structures. These articles compare the optical activity at the 222 nm and the 208 nm wavelength minima. This has often been used to discern between an alpha-helix in solution and a coiled-coil incorporating two or more alpha helices interacting with one another. The articles are presented in the order that is recommended for reading through this literature.

Controlled Formation of Model Homo- and Heterodimer Coiled Coil Polypeptides

Thomas J. Graddis, David G. Myszka, Irwin M. Chaiken

Biochem., 32 12664-12671 (1993).

DOI: 10.1021/bi00210a015