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Myoglobin, energy transfer models

In the present two cases, the results described in Table 7.9 indicate that the rotamers model is not adequate to describe the origin of the fluorescence lifetime of the tryptophans in the two proteins. The shortest fluorescence lifetime (35 or 45 ps) found also for tryptophan residues in myoglobin is an indication of the high energy transfer Forster type from tryptophans to heme. We believe that this lifetime is common or almost all hemoproteins where energy transfer between tryptophan(s) and the heme is very important. [Pg.260]


See other pages where Myoglobin, energy transfer models is mentioned: [Pg.246]    [Pg.296]    [Pg.135]    [Pg.63]    [Pg.1613]    [Pg.158]    [Pg.254]    [Pg.260]    [Pg.1068]    [Pg.1083]   
See also in sourсe #XX -- [ Pg.323 , Pg.325 ]




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