Backbone dynamics of the λ-Cro represser protein determined by15N relaxation measurements. Application of an efficient method for calculation of dynamics parameters

Hiroshi Matsuo; Hiromu Sugeta; Masahiro Shirakawa; Yoshimasa Kyogoku

doi:10.1016/0022-2860(95)09160-2

Backbone dynamics of the λ-Cro represser protein determined by¹⁵N relaxation measurements. Application of an efficient method for calculation of dynamics parameters

Hiroshi Matsuo
, Hiromu Sugeta
, Masahiro Shirakawa
, Yoshimasa Kyogoku

Chemical and Structural Biology (BMBB)

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

4 Scopus citations

Abstract

The backbone dynamics of the λ-Cro represser protein have been studied by analyzing ¹⁵N relaxation rates and the nuclear Overhauser enhancement in terms of a model-free formalism. An efficient method has been developed for obtaining the local motional parameters from the observed data by the least-squares method in which only the overall correlation time can be effectively adjusted as a non-linear parameter. The calculated relaxation parameters of the Cro protein indicated that its C-terminal region corresponding to the DNA binding site is quite mobile.

Original language	English (US)
Pages (from-to)	143-150
Number of pages	8
Journal	Journal of Molecular Structure
Volume	379
Issue number	1-3
DOIs	https://doi.org/10.1016/0022-2860(95)09160-2
State	Published - Jan 1 1996

Keywords

Backbone dynamics
Cro represser
Least squares method
Model-free formalism
N relaxation rate

Publisher link

10.1016/0022-2860(95)09160-2

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Backbone dynamics of the λ-Cro represser protein determined by¹⁵N relaxation measurements. Application of an efficient method for calculation of dynamics parameters. / Matsuo, Hiroshi; Sugeta, Hiromu; Shirakawa, Masahiro et al.
In: Journal of Molecular Structure, Vol. 379, No. 1-3, 01.01.1996, p. 143-150.

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

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AU - Shirakawa, Masahiro

AU - Kyogoku, Yoshimasa

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AB - The backbone dynamics of the λ-Cro represser protein have been studied by analyzing 15N relaxation rates and the nuclear Overhauser enhancement in terms of a model-free formalism. An efficient method has been developed for obtaining the local motional parameters from the observed data by the least-squares method in which only the overall correlation time can be effectively adjusted as a non-linear parameter. The calculated relaxation parameters of the Cro protein indicated that its C-terminal region corresponding to the DNA binding site is quite mobile.

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KW - Least squares method

KW - Model-free formalism

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