Molecular structure of hydrophobins studied with site-directed mutagenesis and vibrational sum-frequency generation spectroscopy

Konrad Meister, Arja Paananen, Bart Speet, Michael Lienemann, Huib Bakker

Research output: Contribution to journalArticleScientificpeer-review

7 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)9398-9402
Number of pages5
JournalThe Journal of Physical Chemistry B
Volume121
Issue number40
DOIs
Publication statusPublished - 12 Oct 2017
MoE publication typeA1 Journal article-refereed

Fingerprint

mutagenesis
Mutagenesis
Vibrational spectra
Molecular structure
molecular structure
Spectroscopy
proteins
Proteins
Aspartic Acid
aspartic acid
Water
spectroscopy
Fungal Proteins
Acids
water
Elasticity
elastic properties
Air
air
1-(heptafluorobutyryl)imidazole

Keywords

  • Air
  • Aspartic Acid/chemistry
  • Elasticity
  • Fungal Proteins/chemistry
  • Hydrophobic and Hydrophilic Interactions
  • Molecular Structure
  • Mutagenesis, Site-Directed
  • Spectrophotometry/methods
  • Surface Properties
  • Trichoderma
  • Vibration
  • Water/chemistry

Cite this

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title = "Molecular structure of hydrophobins studied with site-directed mutagenesis and vibrational sum-frequency generation spectroscopy",
abstract = "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.",
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language = "English",
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pages = "9398--9402",
journal = "The Journal of Physical Chemistry B",
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publisher = "American Chemical Society",
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Molecular structure of hydrophobins studied with site-directed mutagenesis and vibrational sum-frequency generation spectroscopy. / Meister, Konrad; Paananen, Arja; Speet, Bart; Lienemann, Michael; Bakker, Huib.

In: The Journal of Physical Chemistry B, Vol. 121, No. 40, 12.10.2017, p. 9398-9402.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Molecular structure of hydrophobins studied with site-directed mutagenesis and vibrational sum-frequency generation spectroscopy

AU - Meister, Konrad

AU - Paananen, Arja

AU - Speet, Bart

AU - Lienemann, Michael

AU - Bakker, Huib

PY - 2017/10/12

Y1 - 2017/10/12

N2 - 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.

AB - 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.

KW - Air

KW - Aspartic Acid/chemistry

KW - Elasticity

KW - Fungal Proteins/chemistry

KW - Hydrophobic and Hydrophilic Interactions

KW - Molecular Structure

KW - Mutagenesis, Site-Directed

KW - Spectrophotometry/methods

KW - Surface Properties

KW - Trichoderma

KW - Vibration

KW - Water/chemistry

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U2 - 10.1021/acs.jpcb.7b08865

DO - 10.1021/acs.jpcb.7b08865

M3 - Article

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EP - 9402

JO - The Journal of Physical Chemistry B

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