title: Structural characterization of non-native states of sperm whale myoglobin in aqueous ethanol or 2,2,2-trifluoroethanol media.
abstract: The effects of aqueous ethanol or 2,2,2-trifluoroethanol media on the structure of sperm whale myoglobin have been investigated by absorption, CD, and NMR spectra. The structural properties of myoglobin such as heme environments, helix contents, protein folding, and interactions between heme and the protein moiety have been sharply manifested in these spectra. The characterization demonstrated that alcohol-induced conformational change of myoglobin depends on the nature of alcohol and its concentration. It was shown for the first time that, upon the alcohol-induced denaturation of myoglobin, heme is released from partially denatured protein of which helix contents is altered by only about 20% relative to that of native state. Myoglobin has shown to unfold and refold reversibly by controlling the alcohol concentration. Novel methods for the preparation of apomyoglobin and in situ reconstitution of apomyoglobin with heme, based on the alcohol-induced denaturation of the protein, were presented.
authors.affiliation: Department of Chemistry, University of Tsukuba, Tsukuba 305-8571, Japan.
authors.forename: Youhei
authors.initials: Y
authors.lastname: Misumi
authors.forename: Norifumi
authors.initials: N
authors.lastname: Terui
authors.forename: Yasuhiko
authors.initials: Y
authors.lastname: Yamamoto
mesh_terms: D000818:Animals; D001059:Apoproteins / Q000737:chemistry; D002942:Circular Dichroism; D000431:Ethanol / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry* / Q000187:drug effects / Q000302:isolation & purification; D011487:Protein Conformation; D013053:Spectrophotometry; D014270:Trifluoroethanol / Q000494:pharmacology; D014907:Whales
chemical_list: D001059:Apoproteins; D009211:Myoglobin; C010857:apomyoglobin; D000431:Ethanol; D014270:Trifluoroethanol