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Title: Kinetic asymmetry of subunit exchange of homooligomeric protein as revealed by deuteration-assisted small-angle neutron scattering.
Authors: Sugiyama, Masaaki  kyouindb  KAKEN_id  orcid (unconfirmed)
Kurimoto, Eiji
Yagi, Hirokazu
Mori, Kazuhiro  kyouindb  KAKEN_id
Fukunaga, Toshiharu
Hirai, Mitsuhiro
Zaccai, Giuseppe
Kato, Koichi
Author's alias: 杉山, 正明
Issue Date: 19-Oct-2011
Publisher: Elsevier Inc.
Journal title: Biophysical journal
Volume: 101
Issue: 8
Start page: 2037
End page: 2042
Abstract: We developed a novel, to our knowledge, technique for real-time monitoring of subunit exchange in homooligomeric proteins, using deuteration-assisted small-angle neutron scattering (SANS), and applied it to the tetradecamer of the proteasome α7 subunit. Isotopically normal and deuterated tetradecamers exhibited identical SANS profiles in 81% D(2)O solution. After mixing these solutions, the isotope sensitive SANS intensity in the low-q region gradually decreased, indicating subunit exchange, whereas the small-angle x-ray scattering profile remained unchanged confirming the structural integrity of the tetradecamer particles during the exchange. Kinetic analysis of zero-angle scattering intensity indicated that 1), only two of the 14 subunits were exchanged in each tetradecamer and 2), the exchange process involves at least two steps. This study underscores the usefulness of deuteration-assisted SANS, which can provide quantitative information not only on the molecular sizes and shapes of homooligomeric proteins, but also on their kinetic properties.
Rights: © 2011 Biophysical Society. Published by Elsevier
This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
DOI(Published Version): 10.1016/j.bpj.2011.09.004
PubMed ID: 22004758
Appears in Collections:Journal Articles

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