ArticleThe journal of physical chemistry letters2017
Observation of pH-Induced Protein Reorientation at the Water Surface.
Article in The journal of physical chemistry letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- PAS-Domain Protein Orientation at a Polyelectrolyte Surface Revealed by Infrared Nanospectroscopy, Chiral Vibrational Spectroscopy, and Molecular Dynamics Simulations.Biomacromolecules · 2026Article
- True Origin of Amide I Shifts Observed in Protein Spectra Obtained with Sum Frequency Generation Spectroscopy.The journal of physical chemistry letters · 2023Article
- A New Strategy for Reporting Specific Protein Binding Events at Aqueous-Liquid Crystal Interfaces in the Presence of Non-Specific Proteins.ACS applied materials & interfaces · 2020Article
- Ultrafast energy relaxation dynamics of amide I vibrations coupled with protein-bound water molecules.Nature communications · 2019Article
- Hydrophobins: multifunctional biosurfactants for interface engineering.Journal of biological engineering · 2019Review
- Charge-Controlled Surface Properties of Native and Fluorophore-Labeled Bovine Serum Albumin at the Air-Water Interface.The journal of physical chemistry. B · 2018Article
- Molecular Structure of Hydrophobins Studied with Site-Directed Mutagenesis and Vibrational Sum-Frequency Generation Spectroscopy.The journal of physical chemistry. B · 2017Article
- Quantifying biomolecular hydrophobicity: Single molecule force spectroscopy of class II hydrophobins.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.