Molecular Life Sciences

Living Edition
| Editors: Robert D. Wells, Judith S. Bond, Judith Klinman, Bettie Sue Siler Masters, Ellis Bell

Experimental Assessment of Secondary Structure by Circular Dichroism

  • Marina Ramirez-Alvarado
Living reference work entry
DOI: https://doi.org/10.1007/978-1-4614-6436-5_10-2

Synopsis

All proteins in nature have evolved, through selective pressure, to perform specific functions. These functions depend upon their three-dimensional structures arising from sequences of amino acids in the polypeptide chain and adopting secondary structures that interact through long-range interactions within the three-dimensional structure. In this entry, a review of the structure of proteins will be presented as well as the spectroscopic and energetic basis of circular dichroism (CD) utilized extensively to assess secondary structure of proteins.

Introduction

Polypeptide Structure

An amino acid is the basic building block of proteins. All amino acids have a central carbon atom (called Cα) to which a hydrogen atom, an amino group (NH2), and a carboxyl group (COOH) are attached. The major distinction between amino acids lies in the side chain attached to the Cα through the fourth valence. The four groups attached to the Cα atom are chemically different for all the amino acids...

Keywords

Circular Dichroism Circular Dichroism Spectrum Positive Band Negative Band Circular Dichroism Signal 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular BiologyMayo Clinic College of MedicineRochesterUSA