Please use this identifier to cite or link to this item:
|Title:||A hypothetical structural role for proline residues in the flanking segments of protein-protein interaction sites||Authors:||Kini, R.M.
|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|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Sep 14, 2019
WEB OF SCIENCETM
checked on Jul 5, 2019
checked on Sep 6, 2019
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.