From owner-biophys@hgmp.mrc.ac.uk Tue Jun 12 14:52:51 2001 Return-Path: Received: from localhost (localhost [127.0.0.1]) by mercury.hgmp.mrc.ac.uk (Postfix) with ESMTP id 7D0C117BB4 for ; Tue, 12 Jun 2001 14:52:45 +0100 (BST) Received: from localhost (localhost [127.0.0.1]) by mercury.hgmp.mrc.ac.uk (Postfix) with ESMTP id 9D7E217B86 for ; Tue, 12 Jun 2001 14:52:26 +0100 (BST) Received: from niobium.hgmp.mrc.ac.uk (niobium [193.62.192.41]) by mercury.hgmp.mrc.ac.uk (Postfix) with ESMTP id 0D1D917BA4 for ; Tue, 12 Jun 2001 14:51:40 +0100 (BST) Received: (from news@localhost) by niobium.hgmp.mrc.ac.uk (8.9.3+Sun/8.8.8) id OAA25531 for biophys-list@hgmp.mrc.ac.uk; Tue, 12 Jun 2001 14:41:00 +0100 (BST) X-Authentication-Warning: niobium.hgmp.mrc.ac.uk: news set sender to using -f From: "J. Smith" X-Newsgroups: bionet.biophysics Subject: PhD available Cambridge UK Date: Tue, 12 Jun 2001 14:40:57 +0100 Organization: University of Cambridge, England Lines: 65 Message-ID: Mime-Version: 1.0 Content-Type: TEXT/PLAIN; charset=US-ASCII To: biophys@hgmp.mrc.ac.uk Sender: owner-biophys@hgmp.mrc.ac.uk Precedence: bulk Studentship on EPSRC funded research project in structural bio/chemo-informatics - Department of Chemistry, University of Cambridge Title: Novel Computational Approaches to the Understanding and Prediction of Protein-Ligand Interactions Summary: The prediction, design, evolution and energetics of protein-ligand interactions allow a systematic and detailed understanding of binding that will feed into the area of molecular design, particularly in drug design (computational pharmacology). The aim is to understand protein-ligand binding in order to aid the design of new drugs, contribute to the prediction of side effects, the assignment of proteins molecular functions from genetic data, and the annotation of genomes. We will develop a database of protein-ligand interactions containing chemical, biochemical and bioinformatics data. This will be sub-divided into characteristic datasets reflecting different aspects of structure binding and evolution. We will carry out specific studies based on molecular similarity in order to establish correlations between, on the one hand, the structural, sequence and evolutionary relationships between proteins and, on the other hand, the molecular similarities of the ligands they bind. We hope to survey across pairs of protein-ligand complexes in the different characteristic subsets. We will also study interaction type usage in order to determine characteristic patterns in protein-ligand complexes belonging to the characteristic subsets and to cluster the complexes on the basis of these patterns. Training: This will include computational methods, structural biochemistry, chemical biology and research methods. Situated: This projects will be in the Unilever Cambridge Centre for Molecular Informatics, Department of Chemistry. The new building with state of the art facilities opened in December 2000. The centre offers a stimulating and exciting working environment for research in one of the world's leading chemical laboratories. New methods will be devised for creating, manipulating and storing molecular data to deepen our understanding of molecules and their properties and to allow novel in-silico experimentation. Contact: For further information on the Unilever Cambridge Centre for Molecular Informatics look at http://www-ucc.ch.cam.ac.uk/ For further information on the PhD project contact Dr. J.B.O. Mitchell Email: jbom1@cam.ac.uk> Phone: +44-(0)1223-762983. .