Structural evolution of human recombinant alphaB-crystallin under UV irradiation.

Structural evolution of human recombinant alphaB-crystallin under UV irradiation. Research Abstract Details 

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Structural evolution of human recombinant alphaB-crystallin under UV irradiation. Abstract Text:

Masaaki Sugiyama,Noriko Fujii,Yukio Morimoto,Sakie Kurabayashi,Martin E Vigild,Tatsuo Nakagawa,Takashi Sato,Keiji Itoh,Kazuhiro Mori,Toshiharu Fukunaga,

External stresses cause certain proteins to lose their regular structure and aggregate. In order to clarify this abnormal aggregation process, a structural evolution of human recombinant alphaB-crystallin under UV irradiation was observed with in situ small-angle neutron scattering. The abnormal aggregation process was identified to fall in three time zones: incubation, aggregation, and saturation. During the incubation time, the size of aggregates was almost unchanged but a deformation in the local structure was developing. After the incubation time, abnormal aggregation proceed. When the volume of the aggregates reached around twice the size as that of the initial aggregates, the aggregation rate slowed down, which marked the onset of saturation.

Structural evolution of human recombinant alphaB-crystallin under UV irradiation. Publishing Authors By Initials

M Sugiyama,N Fujii,Y Morimoto,S Kurabayashi,ME Vigild,T Nakagawa,T Sato,K Itoh,K Mori,T Fukunaga,

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Structural evolution of human recombinant alphaB-crystallin under UV irradiation. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Biomacromolecules

VOLUME: 9

Page Numbers: 431-4

Journal Abbreviation: Biomacromolecules

ISSN: 1526-4602

DAY: 23

MONTH: 01

YEAR: 2008

Structural evolution of human recombinant alphaB-crystallin under UV irradiation. Information

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LANGUAGE: eng

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AFFILIATION: Research Reactor Institute, Kyoto University, Osaka 590-0494, Japan. sugiyama@rri.kyoto-u.ac.jp

Country: United States

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MEDLINETA: Biomacromolecules

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