Observation of pH-Induced Protein Reorientation at the Water Surface

Konrad Meister (Corresponding Author), Steven J. Roeter, Arja Paananen, Sander Woutersen, Jan Versluis, Géza R. Szilvay, Huib J. Bakker

Research output: Contribution to journalArticleScientificpeer-review

8 Citations (Scopus)

Abstract

Hydrophobins are surface-active proteins that form a hydrophobic, water-repelling film around aerial fungal structures. They have a compact, particle-like structure, in which hydrophilic and hydrophobic regions are spatially separated. This surface property renders them amphiphilic and is reminiscent of synthetic Janus particles. Here we report surface-specific chiral and nonchiral vibrational sum-frequency generation spectroscopy (VSFG) measurements of hydrophobins adsorbed to their natural place of action, the air-water interface. We observe that hydrophobin molecules undergo a reversible change in orientation (tilt) at the interface when the pH is varied. We explain this local orientation toggle from the modification of the interprotein interactions and the interaction of hydrophobin with the water solvent, following the pH-induced change of the charge state of particular amino acids.

Original languageEnglish
Pages (from-to)1772-1776
Number of pages5
JournalThe Journal of Physical Chemistry Letters
Volume8
Issue number8
DOIs
Publication statusPublished - 20 Apr 2017
MoE publication typeA1 Journal article-refereed

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surface water
retraining
proteins
Proteins
Water
water
Janus
Vibrational spectra
surface properties
Surface properties
amino acids
Amino acids
interactions
Spectroscopy
Antennas
Amino Acids
Molecules
air
Air
spectroscopy

Keywords

  • hydophobin
  • HFBII
  • air-water interface
  • interfacial behavior
  • vibrational sum-frequency generation spectroscopy
  • VSFGS

Cite this

Meister, Konrad ; Roeter, Steven J. ; Paananen, Arja ; Woutersen, Sander ; Versluis, Jan ; Szilvay, Géza R. ; Bakker, Huib J. / Observation of pH-Induced Protein Reorientation at the Water Surface. In: The Journal of Physical Chemistry Letters. 2017 ; Vol. 8, No. 8. pp. 1772-1776.
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Observation of pH-Induced Protein Reorientation at the Water Surface. / Meister, Konrad (Corresponding Author); Roeter, Steven J.; Paananen, Arja; Woutersen, Sander; Versluis, Jan; Szilvay, Géza R.; Bakker, Huib J.

In: The Journal of Physical Chemistry Letters, Vol. 8, No. 8, 20.04.2017, p. 1772-1776.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Observation of pH-Induced Protein Reorientation at the Water Surface

AU - Meister, Konrad

AU - Roeter, Steven J.

AU - Paananen, Arja

AU - Woutersen, Sander

AU - Versluis, Jan

AU - Szilvay, Géza R.

AU - Bakker, Huib J.

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AB - Hydrophobins are surface-active proteins that form a hydrophobic, water-repelling film around aerial fungal structures. They have a compact, particle-like structure, in which hydrophilic and hydrophobic regions are spatially separated. This surface property renders them amphiphilic and is reminiscent of synthetic Janus particles. Here we report surface-specific chiral and nonchiral vibrational sum-frequency generation spectroscopy (VSFG) measurements of hydrophobins adsorbed to their natural place of action, the air-water interface. We observe that hydrophobin molecules undergo a reversible change in orientation (tilt) at the interface when the pH is varied. We explain this local orientation toggle from the modification of the interprotein interactions and the interaction of hydrophobin with the water solvent, following the pH-induced change of the charge state of particular amino acids.

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