Projects / Programmes
High resolution NMR study of protein structures and their interactions
| Code |
Science |
Field |
Subfield |
| 1.05.00 |
Natural sciences and mathematics |
Biochemistry and molecular biology |
|
| Code |
Science |
Field |
| P004 |
Natural sciences and mathematics |
Biochemistry, Metabolism |
| P002 |
Natural sciences and mathematics |
Physics |
NMR, tertiary structure, folding, isotopic labeling, stefin, protein inhibitor, propeptide, human cathepsin L, protein complex, proteolysis, relaxation
Researchers (1)
| no. |
Code |
Name and surname |
Research area |
Role |
Period |
No. of publicationsNo. of publications |
| 1. |
06628 |
PhD Roman Jerala |
Biochemistry and molecular biology |
Head |
1998 - 1999 |
1,190 |
Organisations (1)
| no. |
Code |
Research organisation |
City |
Registration number |
No. of publicationsNo. of publications |
| 1. |
0104 |
National Institute of Chemistry |
Ljubljana |
5051592000 |
21,007 |
Abstract
The aim of the project is to study by NMR the tertiary structures of proteins and their interactions with other proteins. Tertiary structure of stefin B will be studied in solution by the combined use of genetic engineering for 15N and 13C labeling and state-of-the-art multidimensional heteronuclear NMR techniques. Relaxation properties of the stefin in solution will be measured and dynamics of the free and proteinase-complexed stefins evaluated in the light of biochemical properties. Conformation of the propeptide of cathepsin L and proteins related to the propeptides of cysteine proteases will be studied by multidimensional NMR as well.
