Chemical and thermal unfolding of calreticulin

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Chemical and thermal unfolding of calreticulin. / Duus, K.; Larsen, N.; Tran, T. A. T.; Güven, E.; Skov, L. K.; Jespersgaard, C; Gajhede, Michael; Houen, Gunnar.

In: Protein and Peptide Letters, Vol. 20, 2013, p. 562-568.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Duus, K, Larsen, N, Tran, TAT, Güven, E, Skov, LK, Jespersgaard, C, Gajhede, M & Houen, G 2013, 'Chemical and thermal unfolding of calreticulin', Protein and Peptide Letters, vol. 20, pp. 562-568.

APA

Duus, K., Larsen, N., Tran, T. A. T., Güven, E., Skov, L. K., Jespersgaard, C., Gajhede, M., & Houen, G. (2013). Chemical and thermal unfolding of calreticulin. Protein and Peptide Letters, 20, 562-568.

Vancouver

Duus K, Larsen N, Tran TAT, Güven E, Skov LK, Jespersgaard C et al. Chemical and thermal unfolding of calreticulin. Protein and Peptide Letters. 2013;20:562-568.

Author

Duus, K. ; Larsen, N. ; Tran, T. A. T. ; Güven, E. ; Skov, L. K. ; Jespersgaard, C ; Gajhede, Michael ; Houen, Gunnar. / Chemical and thermal unfolding of calreticulin. In: Protein and Peptide Letters. 2013 ; Vol. 20. pp. 562-568.

Bibtex

@article{fb90f4ca4b8e4571a10645786000f607,
title = "Chemical and thermal unfolding of calreticulin",
abstract = "Calreticulin is a soluble endoplasmic reticulum chaperone, which has a relatively low melting point due to its remarkable structure with a relatively high content of flexible structural elements. Using far ultraviolet circular dichroism (CD) spectroscopy and a fluorescent dye binding thermal shift assay, we have investigated the chemical and thermal stability of calreticulin. When the chemical stability of calreticulin was assessed, a midpoint for calreticulin unfolding was calculated to 3.0M urea using CD data at 222 nm. Using the fluorescent dye binding thermal shift assay, calreticulin was found to obtain a molten structure in urea concentrations between 1-1.5 M urea, and to unfold/aggregate at high and low pH values. The results demonstrated that the fluorescent dye binding assay could measure the thermal stability of calreticulin in aqueous buffers with results comparable to melting points obtained by other techniques.",
author = "K. Duus and N. Larsen and Tran, {T. A. T.} and E. G{\"u}ven and Skov, {L. K.} and C Jespersgaard and Michael Gajhede and Gunnar Houen",
note = "DOI findes ikke.",
year = "2013",
language = "English",
volume = "20",
pages = "562--568",
journal = "Protein and Peptide Letters",
issn = "0929-8665",
publisher = "Bentham Science Publishers",

}

RIS

TY - JOUR

T1 - Chemical and thermal unfolding of calreticulin

AU - Duus, K.

AU - Larsen, N.

AU - Tran, T. A. T.

AU - Güven, E.

AU - Skov, L. K.

AU - Jespersgaard, C

AU - Gajhede, Michael

AU - Houen, Gunnar

N1 - DOI findes ikke.

PY - 2013

Y1 - 2013

N2 - Calreticulin is a soluble endoplasmic reticulum chaperone, which has a relatively low melting point due to its remarkable structure with a relatively high content of flexible structural elements. Using far ultraviolet circular dichroism (CD) spectroscopy and a fluorescent dye binding thermal shift assay, we have investigated the chemical and thermal stability of calreticulin. When the chemical stability of calreticulin was assessed, a midpoint for calreticulin unfolding was calculated to 3.0M urea using CD data at 222 nm. Using the fluorescent dye binding thermal shift assay, calreticulin was found to obtain a molten structure in urea concentrations between 1-1.5 M urea, and to unfold/aggregate at high and low pH values. The results demonstrated that the fluorescent dye binding assay could measure the thermal stability of calreticulin in aqueous buffers with results comparable to melting points obtained by other techniques.

AB - Calreticulin is a soluble endoplasmic reticulum chaperone, which has a relatively low melting point due to its remarkable structure with a relatively high content of flexible structural elements. Using far ultraviolet circular dichroism (CD) spectroscopy and a fluorescent dye binding thermal shift assay, we have investigated the chemical and thermal stability of calreticulin. When the chemical stability of calreticulin was assessed, a midpoint for calreticulin unfolding was calculated to 3.0M urea using CD data at 222 nm. Using the fluorescent dye binding thermal shift assay, calreticulin was found to obtain a molten structure in urea concentrations between 1-1.5 M urea, and to unfold/aggregate at high and low pH values. The results demonstrated that the fluorescent dye binding assay could measure the thermal stability of calreticulin in aqueous buffers with results comparable to melting points obtained by other techniques.

M3 - Journal article

C2 - 22998950

VL - 20

SP - 562

EP - 568

JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

SN - 0929-8665

ER -

ID: 40766328