The first part of this project involves computer refinement of protein structures determined from X-ray crystallographic data. These researchers are interested in three proteins-the bifunctional enzyme (6-phosphofruto-2-kinase/fructose-2, 6-bisphosphatase), glucokinase, and the glucokinase regulatory protein. These three enzymes are involved in the regulation and control of blood glucose levels. Xplor or CNS is used as the first step in the refinement. Presently, the researchers do not have good crystals from any of these proteins. However, they have now purified large quantities of all three and are trying to crystallize them.
Timothy A. Anderson, Research Associate
Seth T. Gammon, Supercomputing Institute Undergraduate Intern
99/256 |
"The Structure of Vitellogenin Provides a Molecular Model for the Assembly and Secretion of Atherogenic Lipoproteins," C.J. Mann, T.A. Anderson, J. Read, S.A. Chester, G.B. Harrison, S. Köchl, P.J. Ritchie, P. Bradbury, F.S. Hussain, J. Amey, B. Vanloo, Journal of Molecular Biology, 285, p. 391 (1999). |
The second project deals with the development of the graphical software package maid. This package presents a unique approach to the refinement of protein structures based on X-ray crystallographic data. It provides an interface for performing real space molecular dynamics as one builds new structures into the electron density map. An early version of this package has already been published. Recently, a major revision of this package was carried out, and some important new featureswere added. This new version has a new graphical interface that should be more flexible. The main new feature being developed is a procedure for automating the building of protein structure into the electron density map. At present, this is a procedure that requires several weeks to a month of a skilled investigator working on a high performance graphics terminal. The new program has several steps. The first step searches through the entire map, looking for and building in amino acids for regions that are beta sheets or alpha helices. The second step extends these secondary structures into the loop regions. The third step combines the known amino acid sequence data with the tentative amino acids positions to determine the side chain assignment. If the program is successful, it should yield a structure that can be directly input into xplor for refinement.
|
|
URL: http://www.msi.umn.edu/about/publications/annualreport/ar2000/depts/MedSchool/Physiology/levitt.html |
|
| This page last modified on Friday, 30-May-2008 16:14:11 CDT | ||
| Please direct questions or problems to help@msi.umn.edu | ||
|
Website related questions or problems should be directed to
webmaster@msi.umn.edu
The Supercomputing Institute does not collect personal information on visitors to our website. For the University of Minnesota policy, see www.privacy.umn.edu. © 2001 by the Regents of the University of Minnesota |
||