Please use this identifier to cite or link to this item: https://doi.org/10.1006/bbrc.1995.2084
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dc.titleA hypothetical structural role for proline residues in the flanking segments of protein-protein interaction sites
dc.contributor.authorKini, R.M.
dc.contributor.authorEvans, H.J.
dc.date.accessioned2014-11-28T02:12:38Z
dc.date.available2014-11-28T02:12:38Z
dc.date.issued1995
dc.identifier.citationKini, 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
dc.identifier.issn0006291X
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/111714
dc.description.abstractAn 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1006/bbrc.1995.2084
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOSCIENCE CENTRE
dc.description.doi10.1006/bbrc.1995.2084
dc.description.sourcetitleBiochemical and Biophysical Research Communications
dc.description.volume212
dc.description.issue3
dc.description.page1115-1124
dc.description.codenBBRCA
dc.identifier.isiutA1995RL36300055
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