DOI: 10.1073/pnas.87.10.3718. Refinement of protein dynamic structure: normal mode refinement.

Refinement of protein dynamic structure: normal mode refinement.

10.1073/pnas.87.10.3718

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

An x-ray crystallographic refinement method, referred to as the normal mode refinement, is proposed. The Debye-Waller factor is expanded in terms of the effective normal modes whose amplitudes and eigenvectors are experimentally determined by the crystallographic refinement. In contrast to the conventional method, the atomic motions are treated generally as anisotropic and concerted. This method is assessed by using the simulated x-ray data given by a Monte Carlo simulation of human lysozyme. In this article, we refine the dynamic structure by fixing the average static structure to exact coordinates. It is found that the normal mode refinement, using a smaller number of variables, gives a better R factor and more information on the dynamics (anisotropy and collectivity in the motion).

Bibliography

Kidera, A., & Go, N. (1990). Refinement of protein dynamic structure: normal mode refinement. Proceedings of the National Academy of Sciences, 87(10), 3718â3722.

Authors 2

A Kidera (first)
N Go (additional)

References 0 Referenced 84

None

Dates

Type	When
Created	19 years, 2 months ago (May 31, 2006, 7:19 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 12:49 p.m.)
Indexed	2 months, 1 week ago (June 14, 2025, 12:24 a.m.)
Issued	35 years, 3 months ago (May 1, 1990)
Published	35 years, 3 months ago (May 1, 1990)
Published Online	35 years, 3 months ago (May 1, 1990)
Published Print	35 years, 3 months ago (May 1, 1990)

Funders 0

None

BibTeX

@article{Kidera_1990, title={Refinement of protein dynamic structure: normal mode refinement.}, volume={87}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.87.10.3718}, DOI={10.1073/pnas.87.10.3718}, number={10}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Kidera, A and Go, N}, year={1990}, month=may, pages={3718–3722} }

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