ELFT HÍRADÓ

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SZFI SeminarBokor Mónika ZsuzsannaWigner RCP SZFIα-Synuclein proteins ― 
wide-line-NMR melting diagrams and secondary structure predictionsTuesday, 19 
April 2022, 10:00, online, 
https://wigner-hu.zoom.us/j/87921507102?pwd=SjFidU5CT3cvVG1tSFplS0plNXB4UT09  
 Meeting ID: 879 2150 7102  Passcode: 973890The α-synuclein (αS) proteins’ 
structural disorder was measured by ratios of heterogeneous water-binding 
interfaces. They showed the αS monomers, oligomers, and amyloids to possess 
secondary structural elements, although monomers are intrinsically 
disordered. Despite their disordered nature, monomers have 33% secondary 
structure, and therefore they are more compact than a random coil. At the 
lowest potential barriers with mobile hydration water, monomers are already 
functional, a monolayer of mobile hydration water is surrounding them. The 
solvent-accessible surface of the oligomers is ordered or homogenous in its 
interactions with water to 66%. In contrast, αS amyloids are disordered or 
heterogeneous to 75% of their solvent-accessible surface, and both wild type 
and A53T amyloids show identical, low-level hydration. Secondary structure 
predictions of proteins were compared to experimental results by wide-line ¹H 
NMR. αS variants were predicted to be disordered, as in the experiments, but 
the A53T mutant showed less predicted disorder, in contrast with the 
wide-line ¹H NMR result. The last third of the αS variant’s sequence was a 
disordered binding site. β-Sheets are present in αSs, and they extend to more 
amino acid residues in the A53T mutant according to the predictions. The 
latter is verified by experiments. The comparison of the predictions with the 
experiments suggests that helical parts are buried. Minden érdeklődőt 
szívesen látunk! - Everyone is welcome to attend.Róbert 
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