Webbläsaren som du använder stöds inte av denna webbplats. Alla versioner av Internet Explorer stöds inte längre, av oss eller Microsoft (läs mer här: * https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Var god och använd en modern webbläsare för att ta del av denna webbplats, som t.ex. nyaste versioner av Edge, Chrome, Firefox eller Safari osv.

Foto på Anders Irbäck

Anders Irbäck

Professor

Foto på Anders Irbäck

Equilibrium simulation of trp-cage in the presence of protein crowders.

Författare

  • Anna Bille
  • Björn Linse
  • Sandipan Mohanty
  • Anders Irbäck

Summary, in English

While steric crowders tend to stabilize globular proteins, it has been found that protein crowders can have an either stabilizing or destabilizing effect, where a destabilization may arise from nonspecific attractive interactions between the test protein and the crowders. Here, we use Monte Carlo replica-exchange methods to explore the equilibrium behavior of the miniprotein trp-cage in the presence of protein crowders. Our results suggest that the surrounding crowders prevent trp-cage from adopting its global native fold, while giving rise to a stabilization of its main secondary-structure element, an α-helix. With the crowding agent used (bovine pancreatic trypsin inhibitor), the trp-cage-crowder interactions are found to be specific, involving a few key residues, most of which are prolines. The effects of these crowders are contrasted with those of hard-sphere crowders.

Avdelning/ar

  • Beräkningsbiologi och biologisk fysik - Genomgår omorganisation

Publiceringsår

2015

Språk

Engelska

Publikation/Tidskrift/Serie

Journal of Chemical Physics

Volym

143

Issue

17

Dokumenttyp

Artikel i tidskrift

Förlag

American Institute of Physics (AIP)

Ämne

  • Other Physics Topics
  • Biophysics

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 0021-9606