Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin
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چکیده
منابع مشابه
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15 صفحه اولStructure and stability of a second molten globule intermediate in the apomyoglobin folding pathway.
Apomyoglobin folding proceeds through a molten globule intermediate (low-salt form; I1) that has been characterized by equilibrium (pH 4) and kinetic (pH 6) folding experiments. Of the eight alpha-helices in myoglobin, three (A, G, and H) are structured in I1, while the rest appear to be unfolded. Here we report on the structure and stability of a second intermediate, the trichloroacetate form ...
متن کاملStructural characterization of the molten globule state of apomyoglobin by limited proteolysis and HPLC-mass spectrometry.
A method to characterize the structural conformation of an acidic molten globule apomyoglobin (apoMb) at pH 4.2 was developed using limited proteolysis and HPLC-mass spectrometry (HPLC-MS). Endoproteinase Glu-C, which has a double maximum activity at pH 4.0 and pH 7.8 toward glutamic acid (Glu), was used as a proteolytic enzyme. Using this method enabled us to compare the proteolytic cleavages ...
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ژورنال
عنوان ژورنال: Protein Engineering, Design and Selection
سال: 1999
ISSN: 1741-0134,1741-0126
DOI: 10.1093/protein/12.6.485