Human glycine N-methyltransferase is unfolded by urea through a compact monomer state
Human glycine N-methyltransferase is unfolded by urea through a compact monomer state
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DOI：
10.1016/j.abb.2003.09.009
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发表时间：
2003-12-01
影响因子：
3.9
通讯作者：
Wagner, C
中科院分区：
文献类型：
--
作者：
Luka, Z;Wagner, C
Human recombinant glycine N-methyltransferase (GNMT) unfolding by urea was studied by enzyme activity, size-exclusion chromatography, fluorescence spectroscopy, and circular dichroism. Urea unfolding of GNMT is a two-step process. The first transition is a reversible dissociation of the GNMT tetramer to compact monomers in 1.0-3.5 M urea with enzyme inactivation. The compact monomers were characterized by Stokes radius (R-s) of 40.7Angstrom equal to that of globular proteins with the same molecular mass as GNMT monomers, absence of exposure of tryptophan residues into solvent, and presence of about 50% of secondary structure of native protein. The second step of GNMT unfolding is a reversible transition of monomers from compact to a fully unfolded state with R-s of 50Angstrom, exposed tryptophan residues, and disrupted secondary structure in 8 M urea. (C) 2003 Elsevier Inc. All rights reserved.
