The place of inactivated actin and its kinetic predecessor in actin folding - Unfolding

Irina M. Kuznetsova; Olga V. Stepanenko; Olesia V. Stepanenko; Olga I. Povarova; Alexander G. Biktashev; Vladislav V. Verkhusha; Mikhail M. Shavlovsky; Konstantin K. Turoverov

doi:10.1021/bi026412x

The place of inactivated actin and its kinetic predecessor in actin folding - Unfolding

Irina M. Kuznetsova, Olga V. Stepanenko, Olesia V. Stepanenko, Olga I. Povarova, Alexander G. Biktashev, Vladislav V. Verkhusha, Mikhail M. Shavlovsky, Konstantin K. Turoverov

Research output: Contribution to journal › Article › peer-review

50 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	13127-13132
Number of pages	6
Journal	Biochemistry
Volume	41
Issue number	44
DOIs	https://doi.org/10.1021/bi026412x
State	Published - Nov 5 2002
Externally published	Yes

ASJC Scopus subject areas

Biochemistry

Access to Document

10.1021/bi026412x

Cite this

@article{5c36c51c690040e5a92fd4b9aae12567,

title = "The place of inactivated actin and its kinetic predecessor in actin folding - Unfolding",

abstract = "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.",

author = "Kuznetsova, {Irina M.} and Stepanenko, {Olga V.} and Stepanenko, {Olesia V.} and Povarova, {Olga I.} and Biktashev, {Alexander G.} and Verkhusha, {Vladislav V.} and Shavlovsky, {Mikhail M.} and Turoverov, {Konstantin K.}",

year = "2002",

month = nov,

day = "5",

doi = "10.1021/bi026412x",

language = "English (US)",

volume = "41",

pages = "13127--13132",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "44",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=0037027307&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037027307&partnerID=8YFLogxK

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 -

The place of inactivated actin and its kinetic predecessor in actin folding - Unfolding

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this