Please use this identifier to cite or link to this item: https://doi.org/10.1006/bbrc.1995.2084
Title: A hypothetical structural role for proline residues in the flanking segments of protein-protein interaction sites
Authors: Kini, R.M. 
Evans, H.J.
Issue Date: 1995
Citation: Kini, R.M., Evans, H.J. (1995). A hypothetical structural role for proline residues in the flanking segments of protein-protein interaction sites. Biochemical and Biophysical Research Communications 212 (3) : 1115-1124. ScholarBank@NUS Repository. https://doi.org/10.1006/bbrc.1995.2084
Abstract: An examination of more than 1600 protein-protein interaction sites indicated that proline is the residue most commonly found near interaction sites. A structural role is distinguished for these proline residues in the flanking segments of protein-protein interaction sites. The unique nature of proline helps protect the integrity and present the sites, thus promoting protein-protein interactions. A novel approach to the design and development of potent peptide drugs and a simple predictive method to identify protein-protein interaction sites directly from the amino acid sequence have been developed based on this finding. The recognition of this structural role for proline has strong implications for protein chemistry and protein engineering.
Source Title: Biochemical and Biophysical Research Communications
URI: http://scholarbank.nus.edu.sg/handle/10635/111714
ISSN: 0006291X
DOI: 10.1006/bbrc.1995.2084
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