©1996-2019 All Rights Reserved. Online Journal of Bioinformatics . You may not store these pages in any form except for your own personal use. All other usage or distribution is illegal under international copyright treaties. Permission to use any of these pages in any other way besides the  before mentioned must be gained in writing from the publisher. This article is exclusively copyrighted in its entirety to OJB publications. This article may be copied once but may not be, reproduced or  re-transmitted without the express permission of the editors. This journal satisfies the refereeing requirements (DEST) for the Higher Education Research Data Collection (Australia). Linking:To link to this page or any pages linking to this page you must link directly to this page only here rather than put up your own page.


 Online Journal of Bioinformatics © 

 Volume 7 (1) : 32-34, 2006.

Statistical potential determining protein interaction sites


Williams G.


Wolfson Centre for Age Related Diseases, The Wolfson Wing, Hodgkin Building, Kings College London, United Kingdom.




Williams G., Statistical Potential Determining Protein Interaction SitesOnl J Bioinform., 7 (1) : 32-34, 2006. The distribution of interacting residue orientations observed in a database of protein structures is converted into an effective vectorial inter-residue interaction potential. It is argued that this potential can be used to define an effective potential field around a given protein and can be used to predict the proteinís mode of interaction. In particular, probable sites of protein-protein interactions are shown to correspond to low energy clusters of the local energy minima. The protein active site prediction scheme has the possibility of shedding light on protein interactions when, as is most often the case, the protein structure is known but the nature of the interaction is uncertain. Identifying active sites on proteins can lead to the design of small molecule inhibitors either based on the exposed loops neighbouring the given site or based on filling the cavity at the site.

KEY-WORDS : Statistics, Protein Interaction, sites