TY - JOUR
T1 - Compact molten globule-like state of hUBF HMG Box1 at extremely low pH
AU - Zhang, Xuecheng
AU - Zhang, Jiahai
AU - Li, Xuan
AU - Xu, Junjie
AU - Huang, Hongda
AU - Chen, Quan
AU - Wu, Jihui
AU - Shi, Yunyu
N1 - Funding Information:
This work is supported by the Chinese National Fundamental Research Project, Grant G1999075605 and 2002CB713806; the Chinese National Natural Science Foundation, Grant 30270293 and 30121001; the Key Project of the National High Technology Research and Development Program of China, Grant 2002BA711A13; and the Pilot Project of the Knowledge Innovation Program of the Chinese Academy of Science, Grant KSCX1-SW-17.
PY - 2005/4/15
Y1 - 2005/4/15
N2 - Using far and near-UV CD, ANS fluorescence and 2D NMR spectroscopy, an acid-induced partly folded state (A state) at extremely low pH for hUBF HMG Box1 was identified and characterized. As compared to the native state (N), the A state has similar secondary structure, less compact pack with larger amounts of exposed hydrophobic surface, and narrower chemical shift dispersion in 1H-15N HSQC spectrum, which implies that it is a molten globule (MG)-like species. On the other hand, substantial tertiary contacts and cooperative thermal denaturing transition indicate that the A state is closer-relative to the classic MG-to the native folded state. In addition, when the solution pH is adjusted to neutrality, the protein in the A state refolds to the native state easily. All these data suggest that the A state of hUBF HMG Box1 could represent a potential folding intermediate on protein folding pathway.
AB - Using far and near-UV CD, ANS fluorescence and 2D NMR spectroscopy, an acid-induced partly folded state (A state) at extremely low pH for hUBF HMG Box1 was identified and characterized. As compared to the native state (N), the A state has similar secondary structure, less compact pack with larger amounts of exposed hydrophobic surface, and narrower chemical shift dispersion in 1H-15N HSQC spectrum, which implies that it is a molten globule (MG)-like species. On the other hand, substantial tertiary contacts and cooperative thermal denaturing transition indicate that the A state is closer-relative to the classic MG-to the native folded state. In addition, when the solution pH is adjusted to neutrality, the protein in the A state refolds to the native state easily. All these data suggest that the A state of hUBF HMG Box1 could represent a potential folding intermediate on protein folding pathway.
KW - Acid-induced state
KW - Molten globule
KW - Protein folding
KW - hUBF HMG Box1
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U2 - 10.1016/j.bbapap.2004.12.002
DO - 10.1016/j.bbapap.2004.12.002
M3 - Article
C2 - 15752694
AN - SCOPUS:14744283505
SN - 1570-9639
VL - 1748
SP - 66
EP - 73
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
IS - 1
ER -