From owner-biophys@hgmp.mrc.ac.uk Mon Jul 23 14:25:58 2001 Return-Path: Received: from localhost (localhost [127.0.0.1]) by mercury.hgmp.mrc.ac.uk (Postfix) with ESMTP id E8CDE17C10 for ; Mon, 23 Jul 2001 14:25:52 +0100 (BST) Received: from localhost (localhost [127.0.0.1]) by mercury.hgmp.mrc.ac.uk (Postfix) with ESMTP id 6796017BBF for ; Mon, 23 Jul 2001 14:25:37 +0100 (BST) Received: from niobium.hgmp.mrc.ac.uk (niobium [193.62.192.41]) by mercury.hgmp.mrc.ac.uk (Postfix) with ESMTP id 0B14017BE7 for ; Mon, 23 Jul 2001 14:22:54 +0100 (BST) Received: (from news@localhost) by niobium.hgmp.mrc.ac.uk (8.9.3+Sun/8.8.8) id OAA08162 for biophys-list@hgmp.mrc.ac.uk; Mon, 23 Jul 2001 14:12:05 +0100 (BST) X-Authentication-Warning: niobium.hgmp.mrc.ac.uk: news set sender to using -f From: Dong Xu X-Newsgroups: bionet.biophysics Subject: Postdoc position in protein structure modeling/prediction Date: Mon, 23 Jul 2001 09:07:15 -0400 Organization: Oak Ridge National Lab, Oak Ridge, TN Lines: 51 Message-ID: <3B5C2183.76D42D3F@ornl.gov> Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 4.7 [en] (X11; I; SunOS 5.8 sun4u) X-Accept-Language: en To: biophys@hgmp.mrc.ac.uk Sender: owner-biophys@hgmp.mrc.ac.uk Precedence: bulk Postdoc position in protein structure modeling/prediction The Computational Protein Structure Group of Oak Ridge National Laboratory (ORNL) has one opening for a postdoc in protein structure modeling and prediction. The applicants should have a Ph.D. degree in biophysics, computational biology, molecular biology, or computational sciences. Strong ability in computer programming is essential. Background in protein structure modeling and prediction or protein structure determination by NMR is highly desirable. The successful applicant will be involved in the modeling and prediction of the structure of amyloid fibrils. Disease related amyloid fibrils possess a specific, beta-sheet-rich folding motif that is currently obscure because of our inability to use crystallography or high field NMR to determine fibril structure. In this project - a collaboration between ORNL and the University of Tennessee - we will model the structure of the amyloid fibrils associated with Alzheimer's Disease relying both on first principles and on experimental data from the analysis of various aspects of amyloid structure. This well-funded project involves collaboration with the labs of Ron Wetzel (amyloid structure-function), Kelsey Cook (mass spectrometry) and Engin Serpersu (NMR). The general research and development activities of the Group center around four areas: (a) computational methods for protein structure modeling and prediction; (b) hybrid techniques for protein structure determination using computational methods and sparse experimental, e.g. NMR, data; (c) protein complex characterization through modeling and analysis of mass spectrometry data and chemical cross linking; (d) data analysis of large-scale gene and protein expression data. Applicants are invited to submit their CV to Ying Xu Computational Biology Section Building 1060 COM, MS 6480 Oak Ridge National Laboratory Oak Ridge, TN 37831-6480, USA Email: xyn@ornl.gov Web: http://compbio.ornl.gov/~xyn .