Biomedical Engineering Reference
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(1) The modification of and SH groups occurred at a rate that is essentially
lower than that typical for mesophylic proteins. This agrees with the enzyme structural
model showing a solvent exposure of about 1% and 38% for SH and
groups,
respectively.
(2) Arrhenius plots of the spin labels rotation frequency and polarisation of the
fluorescent labels, which are attached to the SH and
groups correspondingly,
exhibit an inflection at
of about 314 K (Fig. 4.4).
The latter point to a conformational transition of the protein at The time-resolved
fluorescence studies indicated that the intrinsic Trp fluorescence emission of the protein
was represented by a bimodal distribution with Lorential shape and was strongly affected
by the protein conformational dynamics (Bismuto et al., 1999; D'Auria et al.,1999).
Parameters of the temperature dependence of the bimodal lifetime distribution, such as
fraction relative intensity, the position of centres, and the distribution line widths,
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