Conformational stability of calreticulin

Research output: Contribution to journalJournal articleResearchpeer-review

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Conformational stability of calreticulin. / Jørgensen, Charlotte S; Trandum, Christa; Larsen, Nanna Brink; Ryder, L Rebekka; Gajhede, Michael; Skov, Lars; Højrup, Peter; Barkholt, Vibeke; Houen, Gunnar.

In: Protein and Peptide Letters, Vol. 12, No. 7, 2005, p. 687-93.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Jørgensen, CS, Trandum, C, Larsen, NB, Ryder, LR, Gajhede, M, Skov, L, Højrup, P, Barkholt, V & Houen, G 2005, 'Conformational stability of calreticulin', Protein and Peptide Letters, vol. 12, no. 7, pp. 687-93.

APA

Jørgensen, C. S., Trandum, C., Larsen, N. B., Ryder, L. R., Gajhede, M., Skov, L., ... Houen, G. (2005). Conformational stability of calreticulin. Protein and Peptide Letters, 12(7), 687-93.

Vancouver

Jørgensen CS, Trandum C, Larsen NB, Ryder LR, Gajhede M, Skov L et al. Conformational stability of calreticulin. Protein and Peptide Letters. 2005;12(7):687-93.

Author

Jørgensen, Charlotte S ; Trandum, Christa ; Larsen, Nanna Brink ; Ryder, L Rebekka ; Gajhede, Michael ; Skov, Lars ; Højrup, Peter ; Barkholt, Vibeke ; Houen, Gunnar. / Conformational stability of calreticulin. In: Protein and Peptide Letters. 2005 ; Vol. 12, No. 7. pp. 687-93.

Bibtex

@article{a3d51311f8ce409686a94267af41c855,
title = "Conformational stability of calreticulin",
abstract = "The conformational stability of calreticulin was investigated. Apparent unfolding temperatures (Tm) increased from 31 degrees C at pH 5 to 51 degrees C at pH 9, but electrophoretic analysis revealed that calreticulin oligomerized instead of unfolding. Structural analyses showed that the single C-terminal alpha-helix was of major importance to the conformational stability of calreticulin.",
keywords = "Calcium, Calorimetry, Differential Scanning, Calreticulin, Cations, Divalent, Circular Dichroism, Humans, Hydrogen-Ion Concentration, Protein Conformation, Protein Denaturation, Protein Folding, Temperature",
author = "J{\o}rgensen, {Charlotte S} and Christa Trandum and Larsen, {Nanna Brink} and Ryder, {L Rebekka} and Michael Gajhede and Lars Skov and Peter H{\o}jrup and Vibeke Barkholt and Gunnar Houen",
year = "2005",
language = "English",
volume = "12",
pages = "687--93",
journal = "Protein and Peptide Letters",
issn = "0929-8665",
publisher = "Bentham Science Publishers",
number = "7",

}

RIS

TY - JOUR

T1 - Conformational stability of calreticulin

AU - Jørgensen, Charlotte S

AU - Trandum, Christa

AU - Larsen, Nanna Brink

AU - Ryder, L Rebekka

AU - Gajhede, Michael

AU - Skov, Lars

AU - Højrup, Peter

AU - Barkholt, Vibeke

AU - Houen, Gunnar

PY - 2005

Y1 - 2005

N2 - The conformational stability of calreticulin was investigated. Apparent unfolding temperatures (Tm) increased from 31 degrees C at pH 5 to 51 degrees C at pH 9, but electrophoretic analysis revealed that calreticulin oligomerized instead of unfolding. Structural analyses showed that the single C-terminal alpha-helix was of major importance to the conformational stability of calreticulin.

AB - The conformational stability of calreticulin was investigated. Apparent unfolding temperatures (Tm) increased from 31 degrees C at pH 5 to 51 degrees C at pH 9, but electrophoretic analysis revealed that calreticulin oligomerized instead of unfolding. Structural analyses showed that the single C-terminal alpha-helix was of major importance to the conformational stability of calreticulin.

KW - Calcium

KW - Calorimetry, Differential Scanning

KW - Calreticulin

KW - Cations, Divalent

KW - Circular Dichroism

KW - Humans

KW - Hydrogen-Ion Concentration

KW - Protein Conformation

KW - Protein Denaturation

KW - Protein Folding

KW - Temperature

M3 - Journal article

C2 - 16522185

VL - 12

SP - 687

EP - 693

JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

SN - 0929-8665

IS - 7

ER -

ID: 40766666