From klein ":at:" cgl.ucsf.EDU Wed Mar 20 14:17:39 1996 Received: from socrates.ucsf.EDU for klein -x- at -x- cgl.ucsf.EDU by www.ccl.net (8.7.1/950822.1) id NAA23164; Wed, 20 Mar 1996 13:27:36 -0500 (EST) From: Received: (from klein;at;localhost) by socrates.ucsf.EDU (8.7.3/GSC4.25) id KAA17467; Wed, 20 Mar 1996 10:27:16 -0800 (PST) Date: Wed, 20 Mar 1996 10:27:16 -0800 (PST) Message-Id: <199603201827.KAA17467*- at -*socrates.ucsf.EDU> To: announce {*at*} santafe.edu, chemistry {*at*} www.ccl.net Subject: Modern Concepts in Macromolecular Modeling (Call for Papers) Call for Papers Modern Concepts in Macromolecular Modeling Pacific Symposium on Biocomputing (http://cgl.ucsf.edu/psb) Ritz-Carlton Kapalua, Maui, Hawaii January 6-9, 1997 Co-chairs Chairs: Jurgen Bajorath, Bristol-Myers Squibb Research Institute Teri E. Klein, University of California, San Francisco The Pacific Symposium on Biocomputing (PSB-97) is an international, multidisciplinary conference for the presentation and discussion of current research in the theory and application of computational methods in problems of biological significance. We are currently soliciting manuscripts for a highly interactive workshop-like session "Modern Concepts in Macromolecular Modeling" and/or abstracts for an accompanying poster session. The session will assess state-of-the-art approaches in the area of macromolecular modeling, in particular protein modeling, to highlight their opportunities, caveats, and limitations. Contributions which introduce or illustrate novel computational methods and which present contemporary applications are equally encouraged. Scientific focal points include: * the development and application of various energy functions for - analysis of the energetics and dynamics of macromolecular structures and their interactions - protein fold recognition - ab initio folding of proteins on the computer - evaluation and assessment of molecular models * techniques to construct protein models in the presence of "twilight zone" sequence similarities such as - analysis of multiple sequences and/or structures - generation of sequence-structure alignments - interactive or automated computer modeling programs Scientific context: While the use of predictive methods to generate and analyze three-dimensional models is increasing, the objectives of such modeling and the problems involved are changing. Classical homology modeling on the basis of significant sequence similarity has more or less introduced macromolecular modeling at times when only a rather limited number of experimentally determined protein structures were available. The scenario has changed dramatically. Many more structures have been determined, and it is a significant task in itself to compare, analyze, and classify these structures. It has become possible to study many intra- and intermolecular interactions in detail, and much effort is currently being spent to understand such interactions in more quantitative energetic terms; be it on the basis of various (free) energy calculations or automated docking procedures. Implications of these studies for drug or protein design are evident. Sequence databases grow at even much faster pace than structural databases, and this is considered a major reason for the increasing interest in modeling. However, popular targets of protein modeling attempts often display, if at all, low or barely detectable sequence similarities to known structures. In these cases, it is difficult to establish structural relationships, even if they exist, and to identify structural templates for modeling. The advent of inverse folding and fold recognition methods has changed the approach to some of these problems. Nevertheless, to apply the results of a fold recognition study, to generate a precise and global sequence-structure alignment, and to actually build a model remains difficult and still requires many subjective decisions. In parallel to novel structure-based or comparative approaches, computational ab initio folding of (small) proteins is, for the first time, successfully performed, albeit at still limited resolution. INSTRUCTIONS FOR AUTHORS PSB '97 will publish peer-reviewed full papers in an archival proceedings. Each accepted paper will be allocated 12 pages in the proceedings volume. Manuscripts adhering to the guidelines set forth on the the PSB web pages will be accepted. Full papers must not have been previously presented or published, nor currently submitted for journal publication. Once accepted to the conference, a paper may be submitted for journal publication. Each manuscript will be refereed by at least four reviewers. Due dates -------------- May 15, 1996 300 word abstract to bajorath #at# protos.bms.com June 15, 1996 Five copies of the manuscript August 15, 1996 Notification of accepted papers September 15, 1996 Accepted camera ready manuscripts Five copies of all full papers must be submitted to: PSB-97 c/o Section on Medical Informatics Stanford University Medical School, MSOB X215 Stanford, CA 94305-5479 USA Authors who do not wish to submit a full paper are welcome to submit 1-2 page abstract adhering to the guidelines set forth on the PSB web pages, which will be distributed at the meeting separately from the archival proceedings. Due dates -------------- May 15, 1996 300 word abstract to bajorath %-% at %-% protos.bms.com August 15, 1996 Notification of accepted abstract/poster September 15, 1996 Accepted camera ready abstract Please send abstracts and questions regarding this session to: Jurgen Bajorath Bristol-Myers Squibb Res. Inst. 3005 First Avenue Seattle, WA 98121 bajorath "-at-" protos.bms.com klein-: at :-cgl.ucsf.edu Tel (206) 727-3612 Fax (206) 727-3602 For more information on the Pacific Symposium on Biocomputing, please see our web site at http://cgl.ucsf.edu/psb or contact: Ms. Sharon Surles PSB Coordinator Interactive Simulations, Inc. 5330 Carroll Canyon Road, Suite 203 San Diego, CA 92121 psb*- at -*intsim.com Phone: +1 (619) 658-9782 FAX: +1 (619) 658-9463