Shape of α-crystallin analyzed by small-angle neutron scattering

Masaaki Sugiyama; Noriko Fujii; Yukio Morimoto; Toshiya Otomo; Shinichi Takata; Masakatsu Misawa; Masahiko Annaka; Keiji Itoh; Kazuhiro Mori; Takashi Sato; Sakie Kurabayashi; Toshiharu Fukunaga

doi:10.1107/S0021889807006838

Shape of α-crystallin analyzed by small-angle neutron scattering

Masaaki Sugiyama, Noriko Fujii, Yukio Morimoto, Toshiya Otomo, Shinichi Takata, Masakatsu Misawa, Masahiko Annaka, Keiji Itoh, Kazuhiro Mori, Takashi Sato, Sakie Kurabayashi, Toshiharu Fukunaga

Physical Chemistry

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

1 Citation (Scopus)

Abstract

The size and shape of aggregates of human recombinant αA-crystallin and αB-crystallin are investigated with small-angle neutron scattering and dynamic light scattering. At a bioactive temperature (310 K), both polypeptides form aggregates with almost the same size and shape. The αB-crystallin maintains an almost identical size and shape at 310 and 288 K, whereas the aggregate of αA-crystallin shows deformation at 288 K. This result suggests that at the lower temperature there is a difference in structural stability between the two aggregates of the polypeptides.

Original language	English
Pages (from-to)	s200-s204
Journal	Journal of Applied Crystallography
Volume	40
Issue number	SUPPL. 1
DOIs	https://doi.org/10.1107/S0021889807006838
Publication status	Published - Apr 2007

All Science Journal Classification (ASJC) codes

Biochemistry, Genetics and Molecular Biology(all)

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10.1107/S0021889807006838

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title = "Shape of α-crystallin analyzed by small-angle neutron scattering",

abstract = "The size and shape of aggregates of human recombinant αA-crystallin and αB-crystallin are investigated with small-angle neutron scattering and dynamic light scattering. At a bioactive temperature (310 K), both polypeptides form aggregates with almost the same size and shape. The αB-crystallin maintains an almost identical size and shape at 310 and 288 K, whereas the aggregate of αA-crystallin shows deformation at 288 K. This result suggests that at the lower temperature there is a difference in structural stability between the two aggregates of the polypeptides.",

author = "Masaaki Sugiyama and Noriko Fujii and Yukio Morimoto and Toshiya Otomo and Shinichi Takata and Masakatsu Misawa and Masahiko Annaka and Keiji Itoh and Kazuhiro Mori and Takashi Sato and Sakie Kurabayashi and Toshiharu Fukunaga",

year = "2007",

month = apr,

doi = "10.1107/S0021889807006838",

language = "English",

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T1 - Shape of α-crystallin analyzed by small-angle neutron scattering

AU - Sugiyama, Masaaki

AU - Fujii, Noriko

AU - Morimoto, Yukio

AU - Otomo, Toshiya

AU - Takata, Shinichi

AU - Misawa, Masakatsu

AU - Annaka, Masahiko

AU - Itoh, Keiji

AU - Mori, Kazuhiro

AU - Sato, Takashi

AU - Kurabayashi, Sakie

AU - Fukunaga, Toshiharu

PY - 2007/4

Y1 - 2007/4

N2 - The size and shape of aggregates of human recombinant αA-crystallin and αB-crystallin are investigated with small-angle neutron scattering and dynamic light scattering. At a bioactive temperature (310 K), both polypeptides form aggregates with almost the same size and shape. The αB-crystallin maintains an almost identical size and shape at 310 and 288 K, whereas the aggregate of αA-crystallin shows deformation at 288 K. This result suggests that at the lower temperature there is a difference in structural stability between the two aggregates of the polypeptides.

AB - The size and shape of aggregates of human recombinant αA-crystallin and αB-crystallin are investigated with small-angle neutron scattering and dynamic light scattering. At a bioactive temperature (310 K), both polypeptides form aggregates with almost the same size and shape. The αB-crystallin maintains an almost identical size and shape at 310 and 288 K, whereas the aggregate of αA-crystallin shows deformation at 288 K. This result suggests that at the lower temperature there is a difference in structural stability between the two aggregates of the polypeptides.

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U2 - 10.1107/S0021889807006838

DO - 10.1107/S0021889807006838

M3 - Article

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VL - 40

SP - s200-s204

JO - Journal of Applied Crystallography

JF - Journal of Applied Crystallography

IS - SUPPL. 1

ER -

Shape of α-crystallin analyzed by small-angle neutron scattering

Abstract

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