|Place of birth||Zagatala, Azerbaijan|
|Date of birth||04.08.1958|
|Education||Baku State University, physics|
|Scientific degree||Doctor of Sciences (“Habilitation” degree) (Physics-Mathematics)|
|Topic of PhD thesis:
- specialty code
- specialty name
- topic name
Thermal physics and molecular physicsFree radical processes under mechanical destruction of fibrous proteins
|Topic of doctoral thesis:
- specialty code
- specialty name
- topic name
Biophysics, ecologyFree radical processes under mechanical destruction of proteins
Election of corresponding member of ANAS:
- specialty name
|Total number of printed scientific publications:
- number of scientific publications printed abroad:
- number of papers published in journals indexed and abstracted in international databases
|Number of patents and certificates of authorship||3|
- number of PhD
- number of Doctor of sciences
|Basic scientific achievements||
1. The initial free radical processes and the chain photo- and thermo-reactions of primary radicals have been determined during the mechanical destruction of proteins. It has been shown that the initial act during the mechanical destruction of proteins is hemolytic breakdown of Calpa-C bonds (1982-1996).
2. Created a new "Site-Directed Tryptophan Fluorescence" (SDTF) method to determine the three-dimensional solution structure of proteins (1997, 2001).
3. The evidence of a scavenging function of tear lipocalin to remove lipids from the human corneal surface (1999, 2005)
4. Tertiary solution structure of the protein called tear lipocalin has been resolved by SDTF that subsequently confirmed by the X-ray analysis of the protein crystal (2005).
5. The ligand binding mechanism, orientation, dynamics and distribution of ligand position inside the cavity of the protein tear lipocalin have been elucidated by SDTF and Site-Directed Spin Labeling methods (2000-2010).
6. We have demonstrated that SDTF provides a promising approach to the study of the solution structure of proteins, as well as pH-dependent conformational dynamics, that is highly complementary
to structural methods such as crystallography. The SDTF method demonstrated that the protonation states of the residues around position 28 modulate conformational switches of the AB loop relevant to ligand binding. (2010).
7. The conserved disulfide bond that links the hairpin CD to the C-terminus may be functionally relevant to all members of the lipocalin family. Deletion of the disulfide bond alters the binding function of the lipocalins in both ligand- and protein-specific manners. (2011)
8. Created a new "Site Directed Circular Dichroism" method to study conformational changes in proteins and demonstrated the advantage of low temperature measurements (2008, 2014).
9. "Cation-pi" interactions in proteins that belong to the lipocaline family have been analyzed to show their structural-functional character (2012)
10. A simple model-free method was developed for direct assessment fluorescent ligand binding by linear spectral summation (2014).
11. In order to evaluate the nearest side chains in proteins, we proposed a method of "double tryptophan exciton" probe that was applied to tear lipocalin (2015)12. SERS (surface enhanced Raman spectroscopy) investigation for whole human blood on a nanostructured ZnO surface indicated that despite the moderate enhancement (20–30 fold), all spectral components of the blood demonstrated in regular Raman are detected in SERS on ZnO. Moreover, SERS on ZnO identifies some components of the blood that are not easily accessible to regular Raman spectroscopy. It has been shown that SERS on ZnO is a valuable tool to investigate the whole blood for diagnosis of various human diseases (2015-2016)
|Names of scientific works||
1. Gasymov O.K., Mamedov Sh.V., and L’vov K.M. Free-radical processes in the mechanical destruction of proteins. Polymer Science USSR, rev. art., 1992, 34, 3, 196-204
2. Gasymov O.K., Abduragimov A.R., Yusifov T.N., Glasgow B.J. Structural changes in human tear lipocalins associated with lipid binding. Biochim.Biophys.Acta, 1998; 1386(1); 145-156.
3. Gasymov O.K., Abduragimov A.R., Yusifov T.N., Glasgow B.J. Resolution of ligand positions by site directed tryptophan fluorescence in tear lipocalin. Protein Science, 2000, 9, 2, 337-343.
4. Gasymov OK, Abduragimov AR, Yusifov TN, Glasgow BJ. Site Directed Tryptophan Fluorescence Reveals the Solution Structure of Tear Lipocalin: Evidence for features that confer promiscuity in ligand binding, Biochemistry, 2001, 40, 14754-14762.
5. Gasymov OK, Abduragimov AR, Prasher P, Yusifov TN and Glasgow BJ. Tear Lipocalin: Evidence for a Scavenging Function to Remove Lipids from the Human Corneal Surface. Invest Ophthalmol Vis Sci., 2005, 43(10), 3165-73.
6. Gasymov OK, Abduragimov AR, Glasgow BG. Intracavitary Ligand Distribution in Tear Lipocalin by Site-Directed Tryptophan Fluorescence, Biochemistry, 2009, 48 (30) 7219-7228.
7. Gasymov OK, Abduragimov AR, Glasgow BG. PH-dependent Conformational Changes in Tear Lipocalin by Site Directed Tryptophan Fluorescence, Biochemistry, 2010, 49 (3), 582-590.
8. Gasymov OK, Abduragimov AR, Glasgow BG. Excited Protein States of Human Tear Lipocalin for Low- and High-Affinity Ligand Binding Revealed by Functional AB Loop Motion, Biophysical Chem, 2010, 149(1-2), 47-57.
9. Gasymov OK, Abduragimov AR, Glasgow BG. Cation-π Interactions in Lipocalins: Structural and Functional Implications, Biochemistry, accelerated publication, 2012, 51(14), 2991-3002.
10. Gasymov OK, Abduragimov AR, Glasgow BG. Double Tryptophan Exciton Probe to Gauge Proximal Side Chains in Proteins- Augmentation at Low Temperature, J Phys Chem B., 2015, 119(10), 3962-3968.
11. Gasymov OK, Alekperov OZ, Aydemirova AH, Kamilova N, Aslanov RB, Bayramov AH, Kerimova A, Surface enhanced Raman scattering of whole human blood on nano-structured ZnO surface, Phys. Status Solidi C, 2017, 1600155
|Membership with international and foreign scientific organizations|
|Pedagogical activity||2001-2012, University of Califormina at Los-Angeles (UCLA); 2016- ANAS, master students|
|Awards and prizes|
|Main place of work and its address||
Institute of Biophysics, 117 Z. Khalilov, Baku, Azerbaijan, AZ1141
|Office phone||(+994 12) 4326248|
|Mobile||(+994 55) 5336648|
|Home phone||(+994 12) 4924814|