LK peptide side chain dynamics at interfaces are independent of secondary structure

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  • Michael A. Donovan, Max Planck Inst Polymer Res, Max Planck Society
  • ,
  • Helmut Lutz, Max Planck Inst Polymer Res, Max Planck Society
  • ,
  • Yeneneh Y. Yimer, Univ Washington, University of Washington, University of Washington Seattle, Dept Chem Engn
  • ,
  • Jim Pfaendtner, Univ Washington, University of Washington, University of Washington Seattle, Dept Chem Engn
  • ,
  • Mischa Bonn, Max Planck Inst Polymer Res, Max Planck Society
  • ,
  • Tobias Weidner

Protein side chain dynamics are critical for specific protein binding to surfaces and protein-driven surface manipulation. At the same time, it is highly challenging to probe side chain motions specifically at interfaces. One important open question is the degree to which the motions of side chains are dictated by local protein folding or by interactions with the surface. Here, we present a real-time measurement of the orientational dynamics of leucine side chains within leucine-lysine (LK) model peptides at the water-air interface, with three representative peptide folds: alpha-helix, 3(10)-helix and beta-strand. The results, modeled and supported bymolecular dynamics simulations, show that the different peptide folds exhibit remarkably similar subpicosecond orientational side chain dynamics at the air/water interface. This demonstrates that the side chain motional dynamics is decoupled from the local secondary structure.

OriginalsprogEngelsk
TidsskriftPhysical Chemistry Chemical Physics
Vol/bind19
Nummer42
Sider (fra-til)28507-28511
Antal sider5
ISSN1463-9076
DOI
StatusUdgivet - 2017

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