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Proteins single molecular protein folding

Myoglobin is a protein of molecular weight of about 17,000 with the protein chain containing 153 amino acid residues folded about the single heme group. This restricts access to the iron atom (by a second heme) and reduces the likelihood of formation of a hematin-like Fe(III) dimer. The micro environment is similar to that in Cytochrome c, but there is no sixth ligand (methionine) to complete the coordination sphere of the iron atom. Thus there is a site to which a dioxygen molecule may reversibly bind. [Pg.95]

Myoglobin is a protein of molecular weight of about 17,000 with the protein chain containing 153 amino acid residues folded about the single haem group. This restricts access to the iron atom (by a second haem) and reduces the likelihood of formation of a... [Pg.43]


See other pages where Proteins single molecular protein folding is mentioned: [Pg.566]    [Pg.385]    [Pg.2]    [Pg.214]    [Pg.146]    [Pg.115]    [Pg.50]    [Pg.148]    [Pg.212]    [Pg.730]    [Pg.68]    [Pg.97]    [Pg.75]    [Pg.42]    [Pg.294]    [Pg.126]    [Pg.737]    [Pg.65]    [Pg.148]    [Pg.309]    [Pg.299]    [Pg.401]    [Pg.284]    [Pg.351]    [Pg.558]    [Pg.274]    [Pg.411]    [Pg.134]    [Pg.120]    [Pg.62]    [Pg.315]    [Pg.172]    [Pg.236]    [Pg.393]    [Pg.1695]    [Pg.706]    [Pg.8]    [Pg.328]    [Pg.417]    [Pg.553]    [Pg.1286]    [Pg.385]    [Pg.724]    [Pg.751]    [Pg.115]   


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