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Statistical Properties of Protein-Protein Interfaces

Department of Structural and Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA
Academic Editor: Louxin Zhang
Received: 13 January 2015 / Revised: 11 March 2015 / Accepted: 30 March 2015 / Published: 2 April 2015
The properties of 1172 protein complexes (downloaded from the Protein Data Bank (PDB)) have been studied based on the concept of circular variance as a buriedness indicator and the concept of mutual proximity as a parameter-free definition of contact. The propensities of residues to be in the protein, on the surface or form contact, as well as residue pairs to form contact were calculated. In addition, the concept of circular variance has been used to compare the ruggedness and shape of the contact surface with the overall surface. View Full-Text
Keywords: accessible surface; circular variance; mutual proximity; residue propensity accessible surface; circular variance; mutual proximity; residue propensity
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MDPI and ACS Style

Mezei, M. Statistical Properties of Protein-Protein Interfaces. Algorithms 2015, 8, 92-99. https://0-doi-org.brum.beds.ac.uk/10.3390/a8020092

AMA Style

Mezei M. Statistical Properties of Protein-Protein Interfaces. Algorithms. 2015; 8(2):92-99. https://0-doi-org.brum.beds.ac.uk/10.3390/a8020092

Chicago/Turabian Style

Mezei, Mihaly. 2015. "Statistical Properties of Protein-Protein Interfaces" Algorithms 8, no. 2: 92-99. https://0-doi-org.brum.beds.ac.uk/10.3390/a8020092

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