Azerbaijan National Academy of Sciences

The first website of Azerbaijan (1995)


Gasymov Oktay Kazim oglu
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) 
Title Professor 
Topic of  PhD thesis:

- specialty code

- specialty name

- topic name

Thermal physics and molecular physics 

Free radical processes under mechanical destruction of fibrous proteins
Topic of doctoral thesis:

- specialty code

- specialty name

- topic name

03.00.02, 03.00.16

Biophysics, ecology

Free radical processes under mechanical destruction of proteins

Election of corresponding member of ANAS:

- date

- 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
Staff training:     

- 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
Other activities  
Awards and prizes  
Main place of work and its address

Institute of Biophysics, 117 Z. Khalilov, Baku, Azerbaijan, AZ1141


General director

Office phone (+994 12) 4326248
Mobile (+994 55) 5336648 
Home phone (+994 12) 4924814 
E-mail oktaygasimov@gmail.comoktaygası