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- Subject: [Fizinfo] Szemináriumok - Seminars: Bokor Mónika Zsuzsanna
- Date: Thu, 14 Apr 2022 06:00:01 +0200 (CEST)
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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
Juhászsem-admin AT szfki.hu
- [Fizinfo] Szemináriumok - Seminars: Bokor Mónika Zsuzsanna, Szeminárium koordinátor, 04/14/2022
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