Purification and structural characterization of human ERp29

ERp29 is a major resident of the endoplasmic reticulum (ER) and is postulated to play an important molecular chaperone role in most animal cells. Human ERp29 was isolated to homogeneity in high yield by using a bacterial expression system. Its secondary structure was studied by circular dichroism (C...

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Bibliographic Details
Published inProtein and peptide letters Vol. 13; no. 8; p. 753
Main Authors Zheng, Jinbiao, Liu, Xingang, Yan, Xiaomin, Dai, Linsen, Ji, Chaoneng
Format Journal Article
LanguageEnglish
Published Netherlands 01.01.2006
Subjects
Amino Acid Sequence
Animals
Circular Dichroism
Electrophoresis, Polyacrylamide Gel
Endoplasmic Reticulum - metabolism
Heat-Shock Proteins - chemistry
Heat-Shock Proteins - genetics
Heat-Shock Proteins - isolation & purification
Humans
Molecular Sequence Data
Protein Structure, Secondary
Rats
Recombinant Proteins - chemistry
Recombinant Proteins - isolation & purification
Spectroscopy, Fourier Transform Infrared
Spectrum Analysis, Raman
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Summary:ERp29 is a major resident of the endoplasmic reticulum (ER) and is postulated to play an important molecular chaperone role in most animal cells. Human ERp29 was isolated to homogeneity in high yield by using a bacterial expression system. Its secondary structure was studied by circular dichroism (CD), Fourier transformed infrared spectroscopy (FTIR) and Raman spectroscopy and it was found that human ERp29 comprises significant alpha-helical structure. The details of its temperature-induced conformational changes was studied by CD and FTIR for the first time, revealing that the protein is stable below 50 degrees C and has two distinct structural transitions between 50 degrees C and 70 degrees C. This may shed light on ERp29's inability to protect substrate proteins against thermal aggregation.
ISSN:0929-8665
DOI:10.2174/092986606777841190