- Strona główna
- O Narodowym Centrum Nauki
- Finansowanie nauki
- Współpraca zagraniczna
- Centrum prasowe
Narodowe Centrum Nauki prezentuje bazę ogłoszeń o wolnych stanowiskach pracy przy projektach finansowanych przez Centrum. Narodowe Centrum Nauki nie ponosi odpowiedzialności za treść i wiarygodność przesyłanych ofert pracy.
Uprzejmie informujemy o nowych warunkach zatrudniania osób na stanowiska typu post-doc: limit czasu upływającego od uzyskania stopnia doktora dla aplikujących na te stanowiska kobiet może być przedłużony o 1,5 roku za każde urodzone bądź przysposobione dziecko.
– Master in Physics/Chemistry/Biology/Computer Sciences or related areas
– Experience with modeling techniques is an advantage
– Experience with Linux environment and scripting is an advantage
– Interest in the interdisciplinary aspect of the project
– Motivation, creativity, liability, ability to work both independently and as a part of the team
– Good command of English
– Molecular docking of glycosaminoglycans and their mimetics
– Molecular dynamics-based analysis of protein-glycosaminoglycan, protein-small molecules, protein-DNA/RNA systems
– Participation in writing publications and presentation of the results at scientific meetings
PhD student position is supposed to be funded by the grant for 3 years with the stipend of 54 000 PLN/year (brutto brutto)Dodatkowe informacje:
Glycosaminoglycans (GAGs) represent a class of linear anionic periodic polysaccharides made up of disaccharide repetitive units containing a hexosamine and an uronic acid. These molecules present varying net degrees and patterns of sulfation. GAGs are major components of the extracellular matrix and play important roles in numerous cellular processes such as signaling, anticoagulation, angiogenesis and communication. Their biological role is executed through intermolecular interactions with protein partners such as growth factors, chemokines, proteases and collagen. Disruptions of protein-GAG interactions can cause a variety of pathologies including cancer, Alzheimer’s and prion diseases, autoimmune and inflammatory disorders. Many of these properties render GAGs promising molecules for the design of new biomaterials in regenerative therapies. At the same time, protein-GAG interactions are still not well characterized at the molecular level. Classical structure determination techniques as well as computational approaches face challenges when dealing with these systems because of GAG’s particular properties as limited availability of experimental structures, extensive length, flexibility, periodicity, symmetry, multipose binding and high variety in the sulfation pattern. The latter is suggested to be crucial for defining their recognition by protein targets and the involvement in particular biochemical processes. Among these challenges, there is one central question in the protein-GAG research field that remains unanswered: How specific are protein-GAG interactions? For several systems, it was shown that the alterations in the GAG type and sulfation pattern changes their protein binding capabilities specifically, whereas for others, it is demonstrated that the only parameter that affects the strength of such interactions is a GAG charge, and so these interactions are completely driven by electrostatics and are, therefore, unspecific. However, there are no systematic studies dealing with the question of protein-GAG specificity. In our project, we aim to get deeper insights into the specificity in protein-GAG interactions by:
1) characterization of the interactions between interleukin-8 (IL-8), a well-known regulatory protein, with GAGs and other negatively charged ligands of different chemical origin (i.e., a series of anionic peptides, DNA, ATPγS, anionic polymers) with different flexibility and charge density which could potentially mimic GAGs;
2) analysis of GAGs interactions with cathepsin B, a protein representing a family of proteases. In spite of featuring the same fold, all members of the cathepsin family interact differently with GAGs in terms of the corresponding complex structures, binding affinities and enzymatic activity impacts of these interactions.
The work will be performed within collaborations with the Research Group of Prof. Daniel Huster (University of Leipzig), in which NMR experiments for these molecular systems will be carried out.
CV and contact data of two referees should be provided to Dr hab. Sergey Samsonov via e-mail firstname.lastname@example.org with the topic “PhD Student, BEETHOVEN CLASSIC” until 30.06.2020