©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.
OJBTM
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.
ABSTRACT
Williams G.,
Statistical Potential Determining Protein Interaction Sites, Onl 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 protein’s
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