Cultural advice

The Australian National University acknowledges, celebrates and pays our respects to the Ngunnawal and Ngambri people of the Canberra region and to all First Nations Australians on whose traditional lands we meet and work, and whose cultures are among the oldest continuing cultures in human history.

Aboriginal and Torres Strait Islander peoples are advised that ANU Library collections may include images, names, voices, and other representations of deceased persons.

Material in the collection may contain terms, language or views that reflect the period in which the item was created and may be considered inappropriate today.

Circular Dichroism Spectroscopy for the Study of Protein-Ligand Interactions

Loading...
Thumbnail Image

Date

Authors

Rodger, Alison
Marrington, Rachel
Roper, David
Windsor, Stuart

Journal Title

Journal ISSN

Volume Title

Publisher

Humana Press Inc.

Access Statement

Research Projects

Organizational Units

Journal Issue

Abstract

Circular dichroism (CD) is the difference in absorption of left and right circularly polarized light, usually by a solution containing the molecules of interest. A signal is only measured for chiral molecules such as proteins. A CD spectrum provides information about the bonds and structures responsible for this chirality. When a small molecule (or ligand) binds to a protein, it acquires an induced CD (ICD) spectrum through chiral perturbation to its structure or electron rearrangements. The wavelengths of this ICD are determined by the ligand’s own absorption spectrum, and the intensity of the ICD spectrum is determined by the strength and geometry of its interaction with the protein. Thus, ICD can be used to probe the binding of ligands to proteins. This chapter outlines protein CD and ICD, together with some of the issues relating to experimental design and implementation.

Description

Citation

Source

Book Title

Methods in Molecular Biology

Entity type

Publication

Access Statement

License Rights

Restricted until