Vliianie gidratatsii na molekuliarno-dinamicheskie svoǐstva syvorotochnogo al'bumina cheloveka v oblasti nizkikh temperatur.

V. R. Bogatyrenko; G. I. Likhtenshteǐn

Vliianie gidratatsii na molekuliarno-dinamicheskie svoǐstva syvorotochnogo al'bumina cheloveka v oblasti nizkikh temperatur.

Translated title of the contribution: Effect of hydration on the molecular dynamic properties of human serum albumin at low temperatures

V. R. Bogatyrenko, G. I. Likhtenshteǐn

Department of Chemistry

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

1 Scopus citations

Abstract

The effect of temperature and hydration on phosphorescence of chromatophores and on saturation curves of ESR spectra of spin labels covalently bound to human serum albumin was studied. It has been shown that at 90-260 degrees K albumin hydration results in intensification of motions of hydrophobic parts with low frequencies (vc less than or equal to 10(3) s-1) and does not affect the motions of hydrophobic and surfacial parts with high frequency.

Translated title of the contribution	Effect of hydration on the molecular dynamic properties of human serum albumin at low temperatures
Original language	Russian
Pages (from-to)	962-966
Number of pages	5
Journal	Biofizika
Volume	30
Issue number	6
State	Published - 1 Nov 1985

ASJC Scopus subject areas

General Medicine

Cite this

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abstract = "The effect of temperature and hydration on phosphorescence of chromatophores and on saturation curves of ESR spectra of spin labels covalently bound to human serum albumin was studied. It has been shown that at 90-260 degrees K albumin hydration results in intensification of motions of hydrophobic parts with low frequencies (vc less than or equal to 10(3) s-1) and does not affect the motions of hydrophobic and surfacial parts with high frequency.",

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N2 - The effect of temperature and hydration on phosphorescence of chromatophores and on saturation curves of ESR spectra of spin labels covalently bound to human serum albumin was studied. It has been shown that at 90-260 degrees K albumin hydration results in intensification of motions of hydrophobic parts with low frequencies (vc less than or equal to 10(3) s-1) and does not affect the motions of hydrophobic and surfacial parts with high frequency.

AB - The effect of temperature and hydration on phosphorescence of chromatophores and on saturation curves of ESR spectra of spin labels covalently bound to human serum albumin was studied. It has been shown that at 90-260 degrees K albumin hydration results in intensification of motions of hydrophobic parts with low frequencies (vc less than or equal to 10(3) s-1) and does not affect the motions of hydrophobic and surfacial parts with high frequency.

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Vliianie gidratatsii na molekuliarno-dinamicheskie svoǐstva syvorotochnogo al'bumina cheloveka v oblasti nizkikh temperatur.

Abstract

ASJC Scopus subject areas

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