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Acid denaturation apomyoglobin

Results from the acidic denaturation of myoglobin as a function of the time. Three species are observed native hMb (heme + myoglobin), denaturated hMb (heme + denaturated hemoglobin) and denaturated aMb (denaturated apomyoglobin). Reproduced (modified) from Konermann L., Rosell F.I., Mauk A.G. and Douglas D.J., Biochemistry, 34, 5554-5559,1997, with permission. [Pg.339]

Yang, A. and B. Honig. (1994). Structural origins of pH and ionic strength effects on protein stability. Acid denaturation of sperm whale apomyoglobin. J. Mol. Biol. 237 602-14. [Pg.234]

Strength Effects on Protein Stability—Acid Denaturation of Sperm Whale Apomyoglobin. [Pg.377]

A.-S. Yang and B. Honig, /. Mol. Biol., 237, 602 (1994). Structural Origins of pH and Ionic Strength Effects on Protein Stability. Acid Denaturation of Sperm WTiale Apomyoglobin. [Pg.310]

Barrick, D., Hughson, F.M., and Baldwin, R.L., 1994, Molecular mechanisms of acid denaturation - the role of histidine residues in the partial unfolding of apomyoglobin, J. Mol Biol. 237 588-601. [Pg.128]

See other pages where Acid denaturation apomyoglobin is mentioned: [Pg.337]    [Pg.337]    [Pg.350]    [Pg.383]    [Pg.44]    [Pg.329]    [Pg.272]    [Pg.322]    [Pg.325]    [Pg.28]    [Pg.273]   
See also in sourсe #XX -- [ Pg.327 , Pg.328 , Pg.329 , Pg.330 ]



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Denaturation apomyoglobin

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