TY - JOUR
T1 - Observation of pH-Induced Protein Reorientation at the Water Surface
AU - Meister, Konrad
AU - Roeters, Steven J.
AU - Paananen, Arja
AU - Woutersen, Sander
AU - Versluis, Jan
AU - Szilvay, Géza R.
AU - Bakker, Huib J.
N1 - Publisher Copyright:
© 2017 American Chemical Society.
PY - 2017/4/20
Y1 - 2017/4/20
N2 - 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.
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.
UR - http://www.scopus.com/inward/record.url?scp=85018484399&partnerID=8YFLogxK
U2 - 10.1021/acs.jpclett.7b00394
DO - 10.1021/acs.jpclett.7b00394
M3 - Article
C2 - 28345915
AN - SCOPUS:85018484399
VL - 8
SP - 1772
EP - 1776
JO - Journal of Physical Chemistry Letters
JF - Journal of Physical Chemistry Letters
IS - 8
ER -