报告题目: The Universe of the flexible molecular systems

报告人: Mariusz Jaremko 副教授

      沙特阿拉伯阿卜杜拉国王科技大学

报告地点:校本部东区生命楼800会议室

报告摘要:

It is widely accepted that macromolecules are very dynamic assemblies experiencing local and global motions in a wide range of time scales spanning from pico-nano seconds to minutes. Proteins are found as folded molecules, having four different levels of structure, primary, secondary, tertiary or quaternary (1-3), intrinsically disordered polypeptide chains (4) or partially folded and disordered at the same time (5). Protein conformation, either ordered or disordered, is often associated with its function (1-5). It is well known that one polypeptide amino acid sequence encodes the presence or absence of a stable structure, however, the conformational equilibrium can be modulated by the environment (3) as well as the interaction with other molecules (1,2,5). However, it is not still well understood how proteins can reach their final conformations and what factors contribute to their miss-folding. Many of diseases are associated with miss-folded proteins, that cannot reach or preserve their native and functional conformation, later turning into toxic oligomers, aggregates, fibril deposits, an hallmark of Parkinson or Alzheimer disease. The presented work focuses on the study of structure and dynamics of folding and miss-folding events of monomeric and oligomeric, folded (3) and unfolded proteins (4, 5), under denaturing conditions (3) or the impact of small molecules (2), by means of modern solution and solid-state state nuclear magnetic resonance (NMR) techniques.

References:

1). High resolution determination of the dynamic structure of membrane proteins (2016) Angew. Chem. Int. Ed. Engl., 35, 10518-10521;

2). Structure of the mitochondrial translocator protein in complex with a diagnostic ligand (2014) Science, 343, 1363-1366;

3). Cold denaturation of a protein dimer monitored at atomic resolution (2013) Nat. Chem. Biol., 9, 264-270;

4). Predictive atomic resolution descriptions of intrinsically disordered hTau40 and α-synuclein in solution from NMR and small angle scattering (2014) Structure, 22, 238-249;

5). Folding of Tau protein on microtubules (2015) Angew. Chem. Int. Ed. Engl., 54, 10347-10351.