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Protein-Protein Interactions: Structurally Conserved Residues Distinguish between Binding Sites and...

Protein-Protein Interactions: Structurally Conserved Residues Distinguish between Binding Sites and...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_201319808

Protein-Protein Interactions: Structurally Conserved Residues Distinguish between Binding Sites and Exposed Protein Surfaces

About this item

Full title

Protein-Protein Interactions: Structurally Conserved Residues Distinguish between Binding Sites and Exposed Protein Surfaces

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2003-05, Vol.100 (10), p.5772-5777

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Polar residue hot spots have been observed at protein-protein binding sites. Here we show that hot spots occur predominantly at the interfaces of macromolecular complexes, distinguishing binding sites from the remainder of the surface. Consequently, hot spots can be used to define binding epitopes. We further show a correspondence between energy ho...

Alternative Titles

Full title

Protein-Protein Interactions: Structurally Conserved Residues Distinguish between Binding Sites and Exposed Protein Surfaces

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_201319808

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_201319808

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1030237100

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