TY - JOUR
T1 - The place of inactivated actin and its kinetic predecessor in actin folding - Unfolding
AU - Kuznetsova, Irina M.
AU - Stepanenko, Olga V.
AU - Stepanenko, Olesia V.
AU - Povarova, Olga I.
AU - Biktashev, Alexander G.
AU - Verkhusha, Vladislav V.
AU - Shavlovsky, Mikhail M.
AU - Turoverov, Konstantin K.
PY - 2002/11/5
Y1 - 2002/11/5
N2 - The kinetics of actin unfolding induced by guanidine hydrochloride of different concentrations was studied. The parametric representation of the kinetic dependencies of tryptophan fluorescence intensity changes recorded at two wavelengths allowed us to detect and characterize a new essentially unfolded kinetic intermediate. Its characteristics suggested that this intermediate state is a premolten globule. It was shown that the equilibrium transition between inactivated and completely unfolded states is also a two-step process and proceeds via an essentially unfolded kinetic intermediate. The new kinetic pathway of actin unfolding - refolding was proposed. According to it, the founded essentially unfolded kinetic state is the on-pathway intermediate, while inactivated actin is the off-pathway misfolded state stabilized by aggregation of partially folded macromolecules of protein.
AB - The kinetics of actin unfolding induced by guanidine hydrochloride of different concentrations was studied. The parametric representation of the kinetic dependencies of tryptophan fluorescence intensity changes recorded at two wavelengths allowed us to detect and characterize a new essentially unfolded kinetic intermediate. Its characteristics suggested that this intermediate state is a premolten globule. It was shown that the equilibrium transition between inactivated and completely unfolded states is also a two-step process and proceeds via an essentially unfolded kinetic intermediate. The new kinetic pathway of actin unfolding - refolding was proposed. According to it, the founded essentially unfolded kinetic state is the on-pathway intermediate, while inactivated actin is the off-pathway misfolded state stabilized by aggregation of partially folded macromolecules of protein.
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U2 - 10.1021/bi026412x
DO - 10.1021/bi026412x
M3 - Article
C2 - 12403613
AN - SCOPUS:0037027307
SN - 0006-2960
VL - 41
SP - 13127
EP - 13132
JO - Biochemistry
JF - Biochemistry
IS - 44
ER -