Denatured collapsed states in protein folding: example of apomyoglobin.
Experimental approaches, including circular dichroism, small angle X-ray scattering, steady-state fluorescence, and fluorescence energy transfer, were applied to study the 3D-structure of apomyolgobin in different conformational states. These included the native and molten globules, along with either less ordered conformations induced by the addition of anions or completely unfolded states. The results show that the partially folded forms of apomyoglobin stabilized by KCl and/or Na(2)SO(4) under unfolding conditions (pH 2) exhibit a significant amount of secondary structure (circular dichroism), low packing density of protein molecules (SAXS), and native-like dimensions of the AGH core (fluorescence energy transfer). This finding indicates that a native-like tertiary fold of the polypeptide chain, i.e., the spatial organization of secondary structure elements, most likely emerges prior to the formation of the molten globule state.
Tcherkasskaya
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Laboratory of Experimental and Computational Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA. tcherkasskaya@nih.gov
Uversky
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D000143:Acids / Q000737:chemistry; D000818:Animals; D000838:Anions / Q000737:chemistry; D001059:Apoproteins / Q000737:chemistry*; D002942:Circular Dichroism; D004735:Energy Transfer; D005453:Fluorescence; D006736:Horses; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry*; D011189:Potassium Chloride / Q000737:chemistry; D011489:Protein Denaturation; D017510:Protein Folding; D014961:X-Ray Diffraction
D000143:Acids; D000838:Anions; D001059:Apoproteins; D009211:Myoglobin; C010857:apomyoglobin; D011189:Potassium Chloride