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Projects / Programmes
High resolution NMR study of protein structures and their interactions
Research activity
| 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 |
Keywords
NMR, tertiary structure, folding, isotopic labeling, stefin, protein inhibitor, propeptide, human cathepsin L, protein complex, proteolysis, relaxation
Evaluation
(metodology)
Citations
Citations for bibliographic records in COBIB.SI that are linked to records in citation databases
Organisations (1) , Researchers (1)
0104 National Institute of Chemistry
| no. | Code | Name and surname | Research area | Role | Period | No. of publicationsNo. of publications |
|---|---|---|---|---|---|---|
| 1. | 06628 | Biochemistry and molecular biology | Head | 1998 - 1999 | 1,267 |
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.