Changes of structure and intramolecular mobility in the course of actin denaturation
IM Kuznetsova, SY Khaitlina, SN Konditerov… - Biophysical …, 1988 - Elsevier
Rabbit skeletal muscle G-actin on heating is transformed into the G t-state in which the
intrinsic fluorescence spectrum is shifted to a longer wavelength compared with that of
native actin, but of much shorter wavelength than that of actin in 8 M urea. A structure with
fluorescence characteristics identical to those of the G t-form appears upon the removal of
Ca 2+, upon partial denaturation in 3–5 M urea and renaturation from the completely
unfolded form in 8 M urea as well as spontaneously during storage of actin solutions. All this …
intrinsic fluorescence spectrum is shifted to a longer wavelength compared with that of
native actin, but of much shorter wavelength than that of actin in 8 M urea. A structure with
fluorescence characteristics identical to those of the G t-form appears upon the removal of
Ca 2+, upon partial denaturation in 3–5 M urea and renaturation from the completely
unfolded form in 8 M urea as well as spontaneously during storage of actin solutions. All this …
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