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...
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Branden C, Tooze J (1999) Introduction to protein structure. 2nd edn. Garland Press. ISBN 0-8153-2305-0. New York, NY
Chothia C (1973) Conformation of twisted beta-pleated sheets in proteins. J Mol Biol 75:295–302
Creighton TE (2010) The physical and chemical basis of molecular biology. Helvetian Press. ISBN 0-9564781-0-8. Distributed by Gardners Books, East Sussex, UK
Jiménez MA, Muñoz V, Rico M, Serrano L (1994) Helix stop and start signals in peptides and proteins. The capping box does not necessarily prevent helix elongation. J Mol Biol 242:487–496
Kelly SM, Price NC (1997) The application of circular dichroism to studies of protein folding and unfolding. Biochim Biophys Acta 1338:161–185
Lewin B (2000) Genes VII. Oxford University Press, Oxford. ISBN 0-19-879276-X
Minor DL Jr, Kim PS (1994) Context is a major determinant of beta-sheet propensity. Nature 371:264–267
Minor DL Jr, Kim PS (1996) Context-dependent secondary structure formation of a designed protein sequence. Nature 380:730–734
Muñoz V, Serrano L (1994) Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales. Proteins 20(4):301–11
Pauling L, Corey RB, Branson HR (1951) The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain. Proc Natl Acad Sci U S A 37:205–211
RamÃrez-Alvarado M, Kortemme T, Blanco FJ, Serrano L (1999) Beta-hairpin and beta-sheet formation in designed linear peptides. Bioorg Med Chem 7(1):93–103
Shellman JA, Schellman C (1964) Conformation of polypeptide chains in Proteins, 2nd edition. Volume 2, In: Neurath H (ed) Academic press, 1–137. Waltham, Massachusetts
Smith CK, Regan L (1995) Guidelines for protein design: the energetics of beta sheet side chain interactions. Science 270:980–982
Woody RW (1996) Circular dichroism and the conformational analysis of biomolecules. In: Fasman GD (ed) Theory of circular dichroism of proteins. Plenum Publishing, New York. ISBN 0-306-45142-5
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer Science+Business Media, LLC
About this entry
Cite this entry
Ramirez-Alvarado, M. (2018). Secondary Structure by Circular Dichroism, Experimental Assessment of. In: Wells, R.D., Bond, J.S., Klinman, J., Masters, B.S.S. (eds) Molecular Life Sciences. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-1531-2_10
Download citation
DOI: https://doi.org/10.1007/978-1-4614-1531-2_10
Published:
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4614-1529-9
Online ISBN: 978-1-4614-1531-2
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences