Peptide folding in the presence of interacting protein crowders

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Abstract

Using Monte Carlo methods, we explore and compare the effects of two protein crowders, BPTI and GB1, on the folding thermodynamics of two peptides, the compact helical trp-cage and the β-hairpin-forming GB1m3. The thermally highly stable crowder proteins are modeled using a fixed backbone and rotatable side-chains, whereas the peptides are free to fold and unfold. In the simulations, the crowder proteins tend to distort the trp-cage fold, while having a stabilizing effect on GB1m3. The extent of the effects on a given peptide depends on the crowder type. Due to a sticky patch on its surface, BPTI causes larger changes than GB1 in the melting properties of the peptides. The observed effects on the peptides stem largely from attractive and specific interactions with the crowder surfaces, and differ from those seen in reference simulations with purely steric crowder particles.

Detaljer

Författare
Enheter & grupper
Externa organisationer
  • Jülich Research Centre
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Biofysik
  • Annan fysik
Originalspråkengelska
Artikelnummer175105
TidskriftJournal of Chemical Physics
Volym144
Utgivningsnummer17
StatusPublished - 2016 maj 7
PublikationskategoriForskning
Peer review utfördJa