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  1. 0 資料タイプ別
  2. 03 紀要論文
  1. 250 大学院医歯学総合研究科(医)
  2. 20 紀要
  3. 01 Acta medica et biologica
  4. Vol.53 No.2

Prediction of the Three-dimensional Structure of Proteins in the Lipid Monolayer on the Basis of a-helix Bundling : The Apolipoprotein B-100 Structure

http://hdl.handle.net/10191/1935
http://hdl.handle.net/10191/1935
8b8ffd4e-4e82-4e05-ae52-16d590029bdc
名前 / ファイル ライセンス アクション
KJ00004161712.pdf KJ00004161712.pdf (1.6 MB)
Item type 紀要論文 / Departmental Bulletin Paper(1)
公開日 2007-05-10
タイトル
タイトル Prediction of the Three-dimensional Structure of Proteins in the Lipid Monolayer on the Basis of a-helix Bundling : The Apolipoprotein B-100 Structure
タイトル
タイトル Prediction of the Three-dimensional Structure of Proteins in the Lipid Monolayer on the Basis of a-helix Bundling : The Apolipoprotein B-100 Structure
言語 en
言語
言語 eng
キーワード
主題Scheme Other
主題 apolipoprotein B-100
キーワード
主題Scheme Other
主題 apolipoprotein A-I
キーワード
主題Scheme Other
主題 a-helix bundle
キーワード
主題Scheme Other
主題 lipid monolayer
キーワード
主題Scheme Other
主題 hydrophobicity
キーワード
主題Scheme Other
主題 lipid- associating motif
資源タイプ
資源 http://purl.org/coar/resource_type/c_6501
タイプ departmental bulletin paper
著者 ZHU, Ying

× ZHU, Ying

WEKO 51822

ZHU, Ying

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OKADA, Masahiko

× OKADA, Masahiko

WEKO 51823

OKADA, Masahiko

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MATSUTO, Takayuki

× MATSUTO, Takayuki

WEKO 51824

MATSUTO, Takayuki

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MIIDA, Takashi

× MIIDA, Takashi

WEKO 51825

MIIDA, Takashi

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抄録
内容記述タイプ Abstract
内容記述 Protein structures profoundly affect their functions. However, strategies for the prediction of protein structures, especially those with complicate intrinsic and extrinsic interactions, remain unsatisfactory. Our present study thus aimed to develop an algorithm to predict the three dimensional structure of membrane proteins on the basis of a-helix bundling. For this purpose, we have taken apolipoprotein B-100 (apoB-100) as an example. Apolipoprotein B-100 is the largest monometric molecule of human plasma proteins, plays an important role in the specific binding of low density lipoprotein (LDL) to the cellsurface receptor, and is strongly correlated with the prevalence of atherosclerosis. Because of its extraordinary size and insoluble nature, its three dimensional structure has been difficult to deduce. In this study, an algorithm was developed based on the consideration that sites of a-helices with higher hydrophilicity are more likely to combine with each other and form bundles in the nonpolar environment. Two cylinder models were established and the interactive force (F) between them was calculated according to hydrophobicity and the charge on the ammo acids. Consequently, a series of values of F ranging from 383 to 7315 was obtained. Extremely high F values, representing areas prone to form bundles, were chosen and analyzed. When regions in close proximity to each other were combined, 5 candidates for a-helix bundles were identified. These regions matched well with the lipid-binding motifs of apoB-100 as reported by others. Multiple helix structures in apolipoprotein A-I were also successfully identified by this program. Thus, the established algorithm is useful in predicting the higher-order structure of apolipoproteins.
書誌情報 Acta medica et biologica
en : Acta medica et biologica

巻 53, 号 2, p. 51-60, 発行日 2005-06
出版者
出版者 Niigata University School of Medicine
ISSN
収録物識別子タイプ ISSN
収録物識別子 05677734
書誌レコードID
収録物識別子タイプ NCID
収録物識別子 AA00508361
著者版フラグ
値 publisher
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ZHU, Ying, OKADA, Masahiko, MATSUTO, Takayuki, MIIDA, Takashi, 2005, Prediction of the Three-dimensional Structure of Proteins in the Lipid Monolayer on the Basis of a-helix Bundling : The Apolipoprotein B-100 Structure: Niigata University School of Medicine, 51–60 p.

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