Probing temperature‐ and solvent‐dependent protein dynamics using terahertz time‐domain spectroscopy

Kasia Tych; Christopher D. Wood; Andrew D.  Burnett; Arwen R. Pearson; Edmund H. Linfield; John E. Cunningham

doi:10.1107/S1600576713029506

Probing temperature‐ and solvent‐dependent protein dynamics using terahertz time‐domain spectroscopy

Kasia Tych, Christopher D. Wood, Andrew D. Burnett, Arwen R. Pearson, Edmund H. Linfield, John E. Cunningham^*

^*Corresponding author voor dit werk

Onderzoeksoutput: Article › Academic › peer review

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The effect of temperature on the terahertz‐frequency‐range material properties of lyophilized and single‐crystal hen egg‐white lysozyme has been measured using terahertz time‐domain spectroscopy, with the results presented and discussed in the context of protein and solvent dynamical and glass transitions. Lyophilized hen egg‐white lysozyme was measured over a temperature range from 4 to 290 K, and a change in the dynamical behaviour of the sample at around 100 K was observed through a change in the terahertz absorption spectrum. Additionally, the effect of cryoprotectants on the temperature‐dependent absorption coefficient is studied, and it is demonstrated that terahertz time‐domain spectroscopy is capable of resolving the true glass transition temperature of single‐crystal hen egg‐white lysozyme at ∼150 K, which is in agreement with literature values measured using differential scanning calorimetry.

Originele taal-2	English
Pagina's (van-tot)	146-153
Aantal pagina's	8
Tijdschrift	Journal of Applied Crystallography
Volume	47
Nummer van het tijdschrift	1
DOI's	https://doi.org/10.1107/S1600576713029506
Status	Published - feb.-2014
Extern gepubliceerd	Ja

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title = "Probing temperature‐ and solvent‐dependent protein dynamics using terahertz time‐domain spectroscopy",

abstract = "The effect of temperature on the terahertz‐frequency‐range material properties of lyophilized and single‐crystal hen egg‐white lysozyme has been measured using terahertz time‐domain spectroscopy, with the results presented and discussed in the context of protein and solvent dynamical and glass transitions. Lyophilized hen egg‐white lysozyme was measured over a temperature range from 4 to 290 K, and a change in the dynamical behaviour of the sample at around 100 K was observed through a change in the terahertz absorption spectrum. Additionally, the effect of cryoprotectants on the temperature‐dependent absorption coefficient is studied, and it is demonstrated that terahertz time‐domain spectroscopy is capable of resolving the true glass transition temperature of single‐crystal hen egg‐white lysozyme at ∼150 K, which is in agreement with literature values measured using differential scanning calorimetry.",

author = "Kasia Tych and Wood, {Christopher D.} and Burnett, {Andrew D.} and Pearson, {Arwen R.} and Linfield, {Edmund H.} and Cunningham, {John E.}",

year = "2014",

month = feb,

doi = "10.1107/S1600576713029506",

language = "English",

volume = "47",

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journal = "Journal of Applied Crystallography",

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publisher = "International Union of Crystallography",

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TY - JOUR

T1 - Probing temperature‐ and solvent‐dependent protein dynamics using terahertz time‐domain spectroscopy

AU - Tych, Kasia

AU - Wood, Christopher D.

AU - Burnett, Andrew D.

AU - Pearson, Arwen R.

AU - Linfield, Edmund H.

AU - Cunningham, John E.

PY - 2014/2

Y1 - 2014/2

N2 - The effect of temperature on the terahertz‐frequency‐range material properties of lyophilized and single‐crystal hen egg‐white lysozyme has been measured using terahertz time‐domain spectroscopy, with the results presented and discussed in the context of protein and solvent dynamical and glass transitions. Lyophilized hen egg‐white lysozyme was measured over a temperature range from 4 to 290 K, and a change in the dynamical behaviour of the sample at around 100 K was observed through a change in the terahertz absorption spectrum. Additionally, the effect of cryoprotectants on the temperature‐dependent absorption coefficient is studied, and it is demonstrated that terahertz time‐domain spectroscopy is capable of resolving the true glass transition temperature of single‐crystal hen egg‐white lysozyme at ∼150 K, which is in agreement with literature values measured using differential scanning calorimetry.

AB - The effect of temperature on the terahertz‐frequency‐range material properties of lyophilized and single‐crystal hen egg‐white lysozyme has been measured using terahertz time‐domain spectroscopy, with the results presented and discussed in the context of protein and solvent dynamical and glass transitions. Lyophilized hen egg‐white lysozyme was measured over a temperature range from 4 to 290 K, and a change in the dynamical behaviour of the sample at around 100 K was observed through a change in the terahertz absorption spectrum. Additionally, the effect of cryoprotectants on the temperature‐dependent absorption coefficient is studied, and it is demonstrated that terahertz time‐domain spectroscopy is capable of resolving the true glass transition temperature of single‐crystal hen egg‐white lysozyme at ∼150 K, which is in agreement with literature values measured using differential scanning calorimetry.

U2 - 10.1107/S1600576713029506

DO - 10.1107/S1600576713029506

M3 - Article

SN - 0021-8898

VL - 47

SP - 146

EP - 153

JO - Journal of Applied Crystallography

JF - Journal of Applied Crystallography

IS - 1

ER -

Probing temperature‐ and solvent‐dependent protein dynamics using terahertz time‐domain spectroscopy

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