Molecular structure of hydrophobins studied with site-directed mutagenesis and vibrational sum-frequency generation spectroscopy
| Autor: | Huib J. Bakker, Bart Speet, Arja Paananen, Konrad Meister, Michael Lienemann |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
Fungal Proteins/chemistry
Stereochemistry Hydrophobin Surface Properties Spectrophotometry/methods 02 engineering and technology 010402 general chemistry 01 natural sciences Vibration Article Protein–protein interaction Fungal Proteins Aspartic Acid/chemistry Amphiphile Molecular film Aspartic acid Materials Chemistry Site-Directed Physical and Theoretical Chemistry Site-directed mutagenesis ta216 ta116 Trichoderma Fungal protein Aspartic Acid Molecular Structure Chemistry Air Water 021001 nanoscience & nanotechnology Elasticity 0104 chemical sciences Surfaces Coatings and Films Spectrophotometry Mutagenesis Water/chemistry Biophysics Mutagenesis Site-Directed 0210 nano-technology Hydrophobic and Hydrophilic Interactions Sum frequency generation spectroscopy |
| Zdroj: | Meister, K, Paananen, A, Speet, B, Lienemann, M & Bakker, H 2017, ' Molecular structure of hydrophobins studied with site-directed mutagenesis and vibrational sum-frequency generation spectroscopy ', The Journal of Physical Chemistry B, vol. 121, no. 40, pp. 9398-9402 . https://doi.org/10.1021/acs.jpcb.7b08865 The Journal of Physical Chemistry. B |
| ISSN: | 1520-5207 1520-6106 |
| DOI: | 10.1021/acs.jpcb.7b08865 |
| Popis: | Hydrophobins are surface-active fungal proteins that adsorb to the water-air interface and self-assemble into amphiphilic, water-repelling films that have a surface elasticity that is an order of magnitude higher than other molecular films. Here we use surface-specific sum-frequency generation spectroscopy (VSFG) and site-directed mutagenesis to study the properties of class I hydrophobin (HFBI) films from Trichoderma reesei at the molecular level. We identify protein specific HFBI signals in the frequency region 1200-1700 cm-1 that have not been observed in previous VSFG studies on proteins. We find evidence that the aspartic acid residue (D30) next to the hydrophobic patch is involved in lateral intermolecular protein interactions, while the two aspartic acid residues (D40, D43) opposite to the hydrophobic patch are primarily interacting with the water solvent. |
| Databáze: | OpenAIRE |
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