Investigation of the micro-structure of the water-protein layer of spin-labelled lysozyme preparations by the method of magnetic relaxation

N. L. Shimanovskii; A. U. Stepanyants; V. P. Lezina; L. V. Ivanov; G. I. Likhtenshtein

Investigation of the micro-structure of the water-protein layer of spin-labelled lysozyme preparations by the method of magnetic relaxation

N. L. Shimanovskii, A. U. Stepanyants, V. P. Lezina, L. V. Ivanov, G. I. Likhtenshtein

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Abstract

Lysozyme was used to analyse the possibilities of the method of magnetic relaxation for investigating the microstructure of the water-protein layer of spin-labelled preparations of proteins and enzymes. It is shown that the effective correlation time of the dipole-dipole interaction of the spin label-water proton complex (τ_c) and also the thermodynamic parameters E_eff and ΔS_eff reflect the local state of the solvate surroundings of lysozyme in the case of labels with long tails. The presence of conformational transitions of lysozyme is demonstrated with change in temperatures (5-80 °C) and as a result of the attachment of the specific inhibitor NAG. It is concluded that the local physical-chemical properties of the water-protein matrix of spin-labelled lysozyme preparations depend on the conformational state of the protein.

Original language	English
Pages (from-to)	840-845
Number of pages	6
Journal	Biophysics (Russian Federation)
Volume	22
Issue number	5
State	Published - 1 Dec 1977
Externally published	Yes

ASJC Scopus subject areas

Biophysics

Cite this

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abstract = "Lysozyme was used to analyse the possibilities of the method of magnetic relaxation for investigating the microstructure of the water-protein layer of spin-labelled preparations of proteins and enzymes. It is shown that the effective correlation time of the dipole-dipole interaction of the spin label-water proton complex (τc) and also the thermodynamic parameters Eeff and ΔSeff reflect the local state of the solvate surroundings of lysozyme in the case of labels with long tails. The presence of conformational transitions of lysozyme is demonstrated with change in temperatures (5-80 °C) and as a result of the attachment of the specific inhibitor NAG. It is concluded that the local physical-chemical properties of the water-protein matrix of spin-labelled lysozyme preparations depend on the conformational state of the protein.",

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T1 - Investigation of the micro-structure of the water-protein layer of spin-labelled lysozyme preparations by the method of magnetic relaxation

AU - Shimanovskii, N. L.

AU - Stepanyants, A. U.

AU - Lezina, V. P.

AU - Ivanov, L. V.

AU - Likhtenshtein, G. I.

PY - 1977/12/1

Y1 - 1977/12/1

N2 - Lysozyme was used to analyse the possibilities of the method of magnetic relaxation for investigating the microstructure of the water-protein layer of spin-labelled preparations of proteins and enzymes. It is shown that the effective correlation time of the dipole-dipole interaction of the spin label-water proton complex (τc) and also the thermodynamic parameters Eeff and ΔSeff reflect the local state of the solvate surroundings of lysozyme in the case of labels with long tails. The presence of conformational transitions of lysozyme is demonstrated with change in temperatures (5-80 °C) and as a result of the attachment of the specific inhibitor NAG. It is concluded that the local physical-chemical properties of the water-protein matrix of spin-labelled lysozyme preparations depend on the conformational state of the protein.

AB - Lysozyme was used to analyse the possibilities of the method of magnetic relaxation for investigating the microstructure of the water-protein layer of spin-labelled preparations of proteins and enzymes. It is shown that the effective correlation time of the dipole-dipole interaction of the spin label-water proton complex (τc) and also the thermodynamic parameters Eeff and ΔSeff reflect the local state of the solvate surroundings of lysozyme in the case of labels with long tails. The presence of conformational transitions of lysozyme is demonstrated with change in temperatures (5-80 °C) and as a result of the attachment of the specific inhibitor NAG. It is concluded that the local physical-chemical properties of the water-protein matrix of spin-labelled lysozyme preparations depend on the conformational state of the protein.

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Investigation of the micro-structure of the water-protein layer of spin-labelled lysozyme preparations by the method of magnetic relaxation

Abstract

ASJC Scopus subject areas

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