Conformational stability of calreticulin

Charlotte S Jørgensen; Christa Trandum; Nanna Brink Larsen; L Rebekka Ryder; Michael Gajhede; Lars Skov; Peter Højrup; Vibeke Barkholt; Gunnar Houen

Conformational stability of calreticulin

Charlotte S Jørgensen, Christa Trandum, Nanna Brink Larsen, L Rebekka Ryder, Michael Gajhede, Lars Skov, Peter Højrup, Vibeke Barkholt, Gunnar Houen

Institut for Kommunikation

7 Citationer (Scopus)

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.

Originalsprog	Engelsk
Tidsskrift	Protein and Peptide Letters
Vol/bind	12
Udgave nummer	7
Sider (fra-til)	687-93
Antal sider	7
ISSN	0929-8665
Status	Udgivet - 2005

Citationsformater

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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",

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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

SN - 0929-8665

VL - 12

SP - 687

EP - 693

JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

IS - 7

ER -

Conformational stability of calreticulin

Abstract

Fingeraftryk

Citationsformater