Projects / Programmes
Folding and Dynamics of Biomolecular Systems
January 1, 1999
- December 31, 2003
| Code |
Science |
Field |
Subfield |
| 1.04.00 |
Natural sciences and mathematics |
Chemistry |
|
| Code |
Science |
Field |
| P351 |
Natural sciences and mathematics |
Structure chemistry |
| P370 |
Natural sciences and mathematics |
Macromolecular chemistry |
| P400 |
Natural sciences and mathematics |
Physical chemistry |
| P410 |
Natural sciences and mathematics |
Theoretical chemistry, quantum chemistry |
| P310 |
Natural sciences and mathematics |
Proteins, enzymology |
| P340 |
Natural sciences and mathematics |
Lipids, steroids, membranes |
Researchers (4)
Organisations (1)
| no. |
Code |
Research organisation |
City |
Registration number |
No. of publicationsNo. of publications |
| 1. |
0104 |
National Institute of Chemistry |
Ljubljana |
5051592000 |
20,997 |
Abstract
Activity of biomolecular systems is intrinsically connected to dynamical processes such as: protein and RNA folding, allosteric changes on receptors, and interactions of various biomolecules with membranes. The dynamics of biomolecular systems is in our laboratory studied by theoretical and experimental methods. The research is focussed on solving the protein folding problem, characterization of physical properties of biologically relevant molecules in solution, and interactions of biomolecules with membranes. The mechanism by which a globular protein folds from denatured state to native conformation is one of the unsolved key problems in protein chemistry. Recently, we have shown that the conformational preferences of amino acid residues is determined by the screening of main chain electrostatic interactions. This electrostatic screening model of conformational preferences is implemented in the algorithm for predicting the three-dimensional structure of one domain proteins. Understanding the dynamics of biopolymer - membrane systems, is crucial for drug design and gene therapy. The mechanism of the biological activity of the antibiotic vancomycin is explored by NMR, vibrational spectroscopy, and molecular modeling. Detailed knowledge of the structure, dynamics and binding interactions will allow the rational design of novel biologically active substances based on vancomycin, which should be important for clinical treatment of life-threatening Gram-positive bacterial infections. The interaction of vancomycin with the membrane, which was discovered in our laboratory, supports the hypothesis that membrane association is important for biological activity by reducing the binding event into a two-dimensional diffusion process. The dynamics of molecular systems DNA - membrane is analyzed with infrared spectroscopy to explore the possibilities for transferring genes into living cells. The description of interaction between DNA and cationic amphiphiles on a molecular level using spectroscopic techniques will assist the understanding of many other important processes involving predominantly electrostatic interaction between charged guest molecule and cell membranes. Infrared spectroscopy is also used to study hydration of proteins, urea and DNA. Stopped and quenched flow methods will be utilized to study the mechanism of the protein folding process in near future. The prospect of predicting the three-dimensional structure of RNA is also examined.
Most important scientific results
Final report
Most important socioeconomically and culturally relevant results
Final report
