[Tryptophan phosphorescence of nascent and inactivated actin at the room temperature].
Millisecond internal dynamics of native and inactivated actin from rabbit skeletal muscle was examined using room temperature phosphorescence. Inactivated actin was prepared by incubation of G-actin at 70 degrees C, by treatment with 4 M urea or 1.5 M guanidinium hydrochloride, renaturation from fully unfolded state or by Ca2+ ion removal. It was shown that inactivation of actin, irrespective of the denaturation procedure applied, leads to a sharp decrease of millisecond fluctuations of the protein structure. Restriction of the slow intramolecular mobility in inactivated actin can result from changes of the protein conformation and/or specific association of macromolecules.
Mazhul'
V M
VM
Institute of Photobiology, National Academy of Sciences of Belarus, ul. Akademicheskaya, 27, Minsk, 220072 Belarus.
Zaĭtseva
E M
EM
Shavlovskiĭ
M M
MM
Kuznetsova
I M
IM
Turoverov
K K
KK
D000199:Actins / Q000737:chemistry*; D000818:Animals; D019791:Guanidine; D007202:Indicators and Reagents; D049449:Luminescence; D018482:Muscle, Skeletal / Q000737:chemistry; D011489:Protein Denaturation; D011817:Rabbits; D013696:Temperature; D014364:Tryptophan / Q000737:chemistry*
D000199:Actins; D007202:Indicators and Reagents; D014364:Tryptophan; D019791:Guanidine
Triptofanovaia fosforestsentsiia pri komnatnoĭ temperature nativnogo i inaktivirovannogo aktina.