Don't miss our weekly PhD newsletter | Sign up now Don't miss our weekly PhD newsletter | Sign up now

  Aggregation of Polyglutamine Tracts Driven by httNT α-helices


   Graduate School of Sciences and Engineering

This project is no longer listed on FindAPhD.com and may not be available.

Click here to search FindAPhD.com for PhD studentship opportunities
  Prof M Sayar  Applications accepted all year round  Funded PhD Project (Students Worldwide)

About the Project

Huntington is a lethal inherited disease with symptoms of a cognitive and psychiatric disorder. It is the most common form of polyglutamine aggregation related diseases. At a molecular level, the disease is associated with the aggregation of polyglutamine tracts resulting from the heavy enzymatic cleavage of Huntingtin. The seventeen amino acid httNT segment, attached to the N-terminal of polyglutamine tract, has a slight tendency towards α-helix structure and is believed to be playing an important role in the aggregation of polyglutamine tracts. In comparison to the dominant β-strand templated protein aggregation mechanism, the α-helix driven aggregation is not commonly seen.

In this project, our primary goal is to use both all-atom and coarse-grained molecular dynamics simulations to test the validity of httNT driven aggregation mechanism of polyglutamine tracts which is based on the current experimental findings. The project will involve both simulations with currently available models and also aim to develop new coarse-grained models which can capture the conformational dynamics and flexibility of the underlying system.

Ph.D. applicants should have a BSc or MSc. in physics, physical chemistry, material science, chemical engineering, or a related field. Prior experience in the field of theory or simulations of soft/biological matter will be an advantage. Applications must include the following documents.
- CV
- Statement of research interests
- Contact details of at least 2 scientific referees
- TOEFL and GRE scores

Applications are only accepted through Koç University’s graduate online application system https://gradapp.ku.edu.tr/login.php. We don’t accept applications or documents via email.

Please check my website for details of our research group activities and members http://home.ku.edu.tr/~msayar/index.html

Funding Notes

Admitted PhD students to the project will receive a full tuition waiver for the PhD program in Computational Sciences and Engineering.

Additional funding for admitted PhD students includes:
- Monthly stipend in Turkish Lira
- Free graduate accommodation on campus or housing stipend
-Health Insurance
- Meal card
- Thesis related travel awards

More details are available on https://gsse.ku.edu.tr/en/admissions/financial-aid-packages/

References

Ozgur, B., & Sayar, M.
Assembly of Triblock Amphiphilic Peptides into One-Dimensional Aggregates and Network Formation
J. Phys. Chem. B 120 (39) , 10243-10257 (2016)
http://pubs.acs.org/doi/full/10.1021/acs.jpcb.6b07545

Dalgicdir, C., Globisch, C. Sayar, M. & Peter, C.
Representing environment-induced helix-coil transitions in a coarse grained peptide model
EPJ-ST 225 (8-9), 1463-1481 (2016)
http://link.springer.com/article/10.1140/epjst/e2016-60147-8

Dalgicdir, C., & Sayar, M.
Conformation and Aggregation of LKalpha14 Peptide in Bulk Water and at the Air/Water Interface
J. Phys. Chem. B 119, 15164-15175 (2015)
http://pubs.acs.org/doi/10.1021/acs.jpcb.5b08871

Dalgicdir, C., Globisch, C., Peter, C., & Sayar, M.
Tipping the Scale from Disorder to Alpha-helix: Folding of Amphiphilic Peptides in the Presence of Macroscopic and Molecular Interfaces.
PLoS Comput. Biol. 11, e1004328 (2015)
http://journals.plos.org/ploscompbiol/article?id=10.1371/journal.pcbi.1004328