Ramin Ekhteiari Salmas
Ramin Ekhteiari Salmas | |
|---|---|
| Add a Photo | |
| Born | May 11, 1980 West Azerbaijan-Urmia |
| Nationality | Iranian. |
| Citizenship | Iran |
| Occupation | Scientist. |
| Academic background | |
| Education | Doctor of Philosophy (Ph.D). |
| Alma mater | King's College London |
| Thesis | Multi-scale Modeling and Investigation of Activation Mechanisms of G Protein-Coupled Receptor. (2015) |
| Academic work | |
| Discipline | Computational Biochemist and Python Developer. |
| Sub-discipline | Molecular Modeling and Molecular Dynamics simulation. |
| Institutions | King's College London. |
| Main interests | Python (programming language). |
| Website | sites |
Dr. Ramin Ekhteiari Salmas, (born May 11, 1980) is an Iranian born scientist who's known for his research on biological systems using molecular modeling and simulation approaches. He's a Python (programming language) developer and studies on protein folding by designing novel statistical mechanics methods.
He was born and raised in West Azerbaijan, Urmia. Salmas received his Ph.D in physical chemistry from Istanbul Technical University in 2015.
Salmas studies on the biological mechanism of dopamine D2 receptor and also their chemical structures.[1][2] Salmas has published more than 50 scientific articles in peer-reviewed journals. He has focused mainly on important protein receptors playing essential roles in drug targets and studied their inhibition and activation mechanisms. One of the critical receptors which is focused in his studies is Dopamine receptor D2 (D2R); the biological conformational changes of D2R were investigated by Salmas and his experimentalist collaborators such as Professor Philip Seeman, who's the discoverer of D2R.[3]
Research
Dopamine receptor D2
In 2018, crystal structure of D2R (PDB id : 6CM4) in an inactive state was reported in binding with an antagonist Risperidone.[4] However, the active form of D2R is still unsolved and studied based on models constructed by comparative methods. In building of the models, not only the trans membrane domains are important, but also the loop domains, particularly the extra-second loop which contributes in the ligand-binding cavity.
References
- ↑ Salmas RE, Seeman P, Stein M, Durdagi S (March 2018). "Structural Investigation of the Dopamine-2 Receptor Agonist Bromocriptine Binding to Dimeric D2HighR and D2LowR States". Journal of chemical information and modeling. 58 (4): 826–836. doi:10.1021/acs.jcim.7b00722.
- ↑ Salmas RE, Seeman P, Aksoydan B, Stein M, Yurtsever M, Durdagi S (January 2017). "Biological Insights of the dopaminergic stabilizer ACR16 at the binding pocket of dopamine D2 receptor". ACS Chemical Neuroscience. 8 (4): 826–836. doi:10.1021/acschemneuro.6b00396.
- ↑ Salmas RE, Seeman P, Aksoydan B, Stein M, Erol I, Kantarcioglu I, Yurtsever M, Durdagi S (March 2017). "Analysis of the Glutamate Agonist LY404, 039 Binding to Nonstatic Dopamine Receptor D2 Dimer Structures and Consensus Docking". ACS Chemical Neuroscience. 8 (6): 1404–1415. doi:10.1021/acschemneuro.7b00070.
- ↑ Wang, Sheng; Che, Tao; Levit, Anat; Shoichet, Brian K.; Wacker, Daniel; Roth, Bryan L. (24 January 2018). "Structure of the D2 dopamine receptor bound to the atypical antipsychotic drug risperidone". Nature. 555 (7695): 269–273. doi:10.1038/nature25758.
External links
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