Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors

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Fourier transform infrared spectrometric analysis of protein conformation : effect of sampling method and stress factors. / van de Weert, Marco; Haris, P I; Hennink, W E; Crommelin, D J.

In: Analytical Biochemistry, Vol. 297, No. 2, 15.10.2001, p. 160-9.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

van de Weert, M, Haris, PI, Hennink, WE & Crommelin, DJ 2001, 'Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors', Analytical Biochemistry, vol. 297, no. 2, pp. 160-9. https://doi.org/10.1006/abio.2001.5337

APA

van de Weert, M., Haris, P. I., Hennink, W. E., & Crommelin, D. J. (2001). Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors. Analytical Biochemistry, 297(2), 160-9. https://doi.org/10.1006/abio.2001.5337

Vancouver

van de Weert M, Haris PI, Hennink WE, Crommelin DJ. Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors. Analytical Biochemistry. 2001 Oct 15;297(2):160-9. https://doi.org/10.1006/abio.2001.5337

Author

van de Weert, Marco ; Haris, P I ; Hennink, W E ; Crommelin, D J. / Fourier transform infrared spectrometric analysis of protein conformation : effect of sampling method and stress factors. In: Analytical Biochemistry. 2001 ; Vol. 297, No. 2. pp. 160-9.

Bibtex

@article{d9186c3bb8564569b84f307d9a147e21,
title = "Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors",
abstract = "Changes in the amide bands in Fourier transform infrared spectra of proteins are generally attributed to alterations in protein secondary structure. In this study spectra of five different globular proteins were compared in the solid and solution states recorded with several sampling techniques. Spectral differences for each protein were observed between the various sampling techniques and physical states, which could not all be explained by a change in protein secondary structure. For example, lyophilization in the absence of lyoprotectants caused spectral changes that could (partially) have been caused by the removal of hydrating water molecules rather than secondary structural changes. Moreover, attenuated total reflectance spectra of proteins in H2O were not directly comparable to transmission spectra due to the anomalous dispersion effect. Our study also revealed that the amide I, II, and III bands differ in their sensitivities to changes in protein conformation: For example, strong bands in the region 1620-1630 and 1685-1695 cm(-1) were seen in the amide I region of aggregated protein spectra. Surprisingly, absorbance of such magnitudes was not observed in the amide II and III region. It appears, therefore, that only the amide I can be used to distinguish between intra- and intermolecular beta-sheet formation. Considering the differing sensitivity of the different amide modes to structural changes, it is advisable to utilize not only the amide I band, but also the amide II and III bands, to determine changes in protein secondary structure. Finally, it is important to realize that changes in these bands may not always correspond to secondary structural changes of the proteins.",
author = "{van de Weert}, Marco and Haris, {P I} and Hennink, {W E} and Crommelin, {D J}",
note = "Copyright 2001 Academic Press.",
year = "2001",
month = "10",
day = "15",
doi = "10.1006/abio.2001.5337",
language = "English",
volume = "297",
pages = "160--9",
journal = "Analytical Biochemistry",
issn = "0003-2697",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Fourier transform infrared spectrometric analysis of protein conformation

T2 - effect of sampling method and stress factors

AU - van de Weert, Marco

AU - Haris, P I

AU - Hennink, W E

AU - Crommelin, D J

N1 - Copyright 2001 Academic Press.

PY - 2001/10/15

Y1 - 2001/10/15

N2 - Changes in the amide bands in Fourier transform infrared spectra of proteins are generally attributed to alterations in protein secondary structure. In this study spectra of five different globular proteins were compared in the solid and solution states recorded with several sampling techniques. Spectral differences for each protein were observed between the various sampling techniques and physical states, which could not all be explained by a change in protein secondary structure. For example, lyophilization in the absence of lyoprotectants caused spectral changes that could (partially) have been caused by the removal of hydrating water molecules rather than secondary structural changes. Moreover, attenuated total reflectance spectra of proteins in H2O were not directly comparable to transmission spectra due to the anomalous dispersion effect. Our study also revealed that the amide I, II, and III bands differ in their sensitivities to changes in protein conformation: For example, strong bands in the region 1620-1630 and 1685-1695 cm(-1) were seen in the amide I region of aggregated protein spectra. Surprisingly, absorbance of such magnitudes was not observed in the amide II and III region. It appears, therefore, that only the amide I can be used to distinguish between intra- and intermolecular beta-sheet formation. Considering the differing sensitivity of the different amide modes to structural changes, it is advisable to utilize not only the amide I band, but also the amide II and III bands, to determine changes in protein secondary structure. Finally, it is important to realize that changes in these bands may not always correspond to secondary structural changes of the proteins.

AB - Changes in the amide bands in Fourier transform infrared spectra of proteins are generally attributed to alterations in protein secondary structure. In this study spectra of five different globular proteins were compared in the solid and solution states recorded with several sampling techniques. Spectral differences for each protein were observed between the various sampling techniques and physical states, which could not all be explained by a change in protein secondary structure. For example, lyophilization in the absence of lyoprotectants caused spectral changes that could (partially) have been caused by the removal of hydrating water molecules rather than secondary structural changes. Moreover, attenuated total reflectance spectra of proteins in H2O were not directly comparable to transmission spectra due to the anomalous dispersion effect. Our study also revealed that the amide I, II, and III bands differ in their sensitivities to changes in protein conformation: For example, strong bands in the region 1620-1630 and 1685-1695 cm(-1) were seen in the amide I region of aggregated protein spectra. Surprisingly, absorbance of such magnitudes was not observed in the amide II and III region. It appears, therefore, that only the amide I can be used to distinguish between intra- and intermolecular beta-sheet formation. Considering the differing sensitivity of the different amide modes to structural changes, it is advisable to utilize not only the amide I band, but also the amide II and III bands, to determine changes in protein secondary structure. Finally, it is important to realize that changes in these bands may not always correspond to secondary structural changes of the proteins.

U2 - 10.1006/abio.2001.5337

DO - 10.1006/abio.2001.5337

M3 - Journal article

C2 - 11673883

VL - 297

SP - 160

EP - 169

JO - Analytical Biochemistry

JF - Analytical Biochemistry

SN - 0003-2697

IS - 2

ER -

ID: 45184839