Iskra Staneva

TL;DR: The probability of finding turns centered in the 25-30 region, where there is a loop in Aβ fibrils, is found to increase upon dimerization and to correlate with experimentally measured rates of fibril formation for the different Aβ42 variants.

TL;DR: The results highlight the importance of overall physical properties of IDP segments, such as net charge or presence of strongly hydrophobic amino acids, for molecular recognition via coupled folding-binding in order to facilitate signaling in a many-to-one manner.

TL;DR: An effective all-atom energy function centering on hydrophobicity, hydrogen bonding, and electrostatic interactions is developed and applied to PDZ domain-peptide interactions, finding a significant diversity among bound peptide conformations for several PDZ domains.

TL;DR: The peptide binding process of PDZ domains, a large PRD family, is explored from an equilibrium perspective using an all-atom Monte Carlo (MC) approach and results are consistent with a binding mechanism in which the peptide C terminal residue binds in an initial, rate-limiting step.