Identification of the response of protein N-H vibrations in vibrational sum-frequency generation spectroscopy of aqueous protein films

Konrad Meister (Corresponding Author), Arja Paananen, Huib Bakker

Research output: Contribution to journalArticleScientificpeer-review

3 Citations (Scopus)

Abstract

The N-H stretching vibration is an important probe for investigating structural and functional properties of proteins but is often difficult to analyze as it overlaps with the O-H stretching vibration of water molecules. In this work we investigate the N-H signals of hydrophobins using conventional (VSFG) and heterodyne-detected vibrational sum-frequency generation spectroscopy (HD-VSDG). Hydrophobins represent a group of surface active proteins that form highly-ordered protein films at the water-air interface and that give rise to prominent vibrational modes. We find that in conventional VSFG spectra N-H specific signals show significant changes in shape and intensity upon altering the pH values. These changes can easily be misinterpreted for conformational changes of the protein. Using HD-VSFG experiments, we demonstrate, that for hydrophobin films the change of the N-H response with pH can be well explained from the interference of the N-H response with the broad interfacial water O-H stretch band.
Original languageEnglish
Pages (from-to)10804-10807
Number of pages4
JournalPhysical Chemistry Chemical Physics
Volume19
Issue number17
DOIs
Publication statusPublished - 1 Jan 2017
MoE publication typeA1 Journal article-refereed

Fingerprint

Vibrational spectra
Spectroscopy
proteins
vibration
spectroscopy
Stretching
Water
Proteins
water
vibration mode
interference
Molecules
probes
air
Air
molecules
Experiments

Keywords

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

Cite this

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abstract = "The N-H stretching vibration is an important probe for investigating structural and functional properties of proteins but is often difficult to analyze as it overlaps with the O-H stretching vibration of water molecules. In this work we investigate the N-H signals of hydrophobins using conventional (VSFG) and heterodyne-detected vibrational sum-frequency generation spectroscopy (HD-VSDG). Hydrophobins represent a group of surface active proteins that form highly-ordered protein films at the water-air interface and that give rise to prominent vibrational modes. We find that in conventional VSFG spectra N-H specific signals show significant changes in shape and intensity upon altering the pH values. These changes can easily be misinterpreted for conformational changes of the protein. Using HD-VSFG experiments, we demonstrate, that for hydrophobin films the change of the N-H response with pH can be well explained from the interference of the N-H response with the broad interfacial water O-H stretch band.",
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Identification of the response of protein N-H vibrations in vibrational sum-frequency generation spectroscopy of aqueous protein films. / Meister, Konrad (Corresponding Author); Paananen, Arja; Bakker, Huib.

In: Physical Chemistry Chemical Physics, Vol. 19, No. 17, 01.01.2017, p. 10804-10807.

Research output: Contribution to journalArticleScientificpeer-review

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T1 - Identification of the response of protein N-H vibrations in vibrational sum-frequency generation spectroscopy of aqueous protein films

AU - Meister, Konrad

AU - Paananen, Arja

AU - Bakker, Huib

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Y1 - 2017/1/1

N2 - The N-H stretching vibration is an important probe for investigating structural and functional properties of proteins but is often difficult to analyze as it overlaps with the O-H stretching vibration of water molecules. In this work we investigate the N-H signals of hydrophobins using conventional (VSFG) and heterodyne-detected vibrational sum-frequency generation spectroscopy (HD-VSDG). Hydrophobins represent a group of surface active proteins that form highly-ordered protein films at the water-air interface and that give rise to prominent vibrational modes. We find that in conventional VSFG spectra N-H specific signals show significant changes in shape and intensity upon altering the pH values. These changes can easily be misinterpreted for conformational changes of the protein. Using HD-VSFG experiments, we demonstrate, that for hydrophobin films the change of the N-H response with pH can be well explained from the interference of the N-H response with the broad interfacial water O-H stretch band.

AB - The N-H stretching vibration is an important probe for investigating structural and functional properties of proteins but is often difficult to analyze as it overlaps with the O-H stretching vibration of water molecules. In this work we investigate the N-H signals of hydrophobins using conventional (VSFG) and heterodyne-detected vibrational sum-frequency generation spectroscopy (HD-VSDG). Hydrophobins represent a group of surface active proteins that form highly-ordered protein films at the water-air interface and that give rise to prominent vibrational modes. We find that in conventional VSFG spectra N-H specific signals show significant changes in shape and intensity upon altering the pH values. These changes can easily be misinterpreted for conformational changes of the protein. Using HD-VSFG experiments, we demonstrate, that for hydrophobin films the change of the N-H response with pH can be well explained from the interference of the N-H response with the broad interfacial water O-H stretch band.

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