alexa Expanding the Loop Segments in β-hairpin Nonapeptides in Protein Folding and Biological Functions
ISSN: 2329-8936

Transcriptomics: Open Access
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Editorial

Expanding the Loop Segments in β-hairpin Nonapeptides in Protein Folding and Biological Functions

Rajagopal Appavu*
Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, Texas, United States Minor Outlying Islands
*Corresponding Author : Rajagopal Appavu
Experimental Radiation Oncology
The University of Texas MD Anderson Cancer Center
1515 Holcombe Blvd, Y6.6006 Houston
Texas 77030, United States Minor Outlying Islands
Tel: 409-256-9987
Fax: 713-794-5369
E-mail: [email protected]
Received January 28, 2016; Accepted February 18, 2016; Published February 23, 2016
Citation: Appavu R (2016) Expanding the Loop Segments in β-hairpin Nonapeptides in Protein Folding and Biological Functions. Transcriptomics 4:e116. doi:10.4172/2329-8936.1000e116
Copyright: © 2016 Appavu R. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

 

 

Abstract

Analysis of β-hairpins in proteins, have revealed several examples of antiparallel β-strands connected by short linking segments, which contain more than two residues.The design of synthetic peptide hairpins formed with central two residue turns has been facilitated by the ease with which specific types of β-turn structures can be generated in short peptides. Earlier work in this laboratory has addressed the question of expanding the central connecting loop in designed peptide β-hairpins.

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