Speaker
Jana Aupic
(National Institute of Chemistry)
Description
One of the approaches to designing new protein folds relies on using modular building blocks, e.g. coiled-coils that interact only with their cognate pair in a well-understood fashion. A recent result of this kind of design strategy is a tetrahedron constructed from a single polypeptide chain composed of six pairs of coiled-coil forming segments[1]. The order of segments in a protein sequence that leads to a desired polyhedral structure is not unique. Since the kinetics and folding pathway are largely determined by the sequence of modules, topological considerations should be taken into account when designing protein polyhedra[2]. To investigate what governs the folding process, different topologies that allow a single polypeptide chain to fold into a tetrahedron were examined using structure-based (Gō) simulations. Obtained folding pathways were compared to results of simple deterministic folding, where segment pairs that are closest together form first.
References:
[1] Gradišar H. et al. (2013) Nat. Chem. Biol., 9, 362-6.
[2] Koga N. and Takada S. (2001) J. Mol. Biol., 313, 171–180.
Primary author
Jana Aupic
(National Institute of Chemistry)
Co-authors
Dr
Ajasja Ljubetič
(National Institute of Chemistry)
Dr
Igor Drobnak
(National Institute of Chemistry)
Prof.
Roman Jerala
(National Institute of Chemistry, EN-FIST Centre of excellence)
