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ツゲ ヒデアキ
TSUGE HIDEAKI
津下 英明 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2009/07 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Non-native alpha-helix formation is not necessary for folding of lipocalin: Comparison of burst-phase folding between tear lipocalin and beta-lactoglobulin |
| 執筆形態 | その他 |
| 掲載誌名 | PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS |
| 出版社・発行元 | WILEY-LISS |
| 巻・号・頁 | 76(1),pp.226-236 |
| 著者・共著者 | Seiichi Tsukamoto,Takako Yamashita,Yoshiteru Yamada,Kazuo Fujiwara,Kosuke Maki,Kunihiro Kuwajima,Yoshitaka Matsumura,Hiroshi Kihara,Hideaki Tsuge,Masamichi Ikeguchi |
| 概要 | Tear lipocalin and beta-lactoglobulin are members of the lipocalin superfamily. They have similar tertiary structures but unusually low overall sequence similarity. Non-native helical structures are formed during the early stage of beta-lactoglobulin folding. To address whether the non-native helix formation is found in the folding of other lipocalin superfamily proteins, the folding kinetics of a tear lipocalin variant were investigated by stoppedflow methods measuring the time-dependent changes in circular dichroism (CD) spectrum and small-angle X-ray scattering (SAXS). CD spectrum showed that extensive secondary structures are not formed during a burst-phase (within a measurement dead time). The SAXS data showed that the radius of gyration becomes much smaller than in the unfolded state during the burst-phase, indicating that the molecule is collapsed during an early stage of folding. Therefore, non-native helix formation is not general for folding of all lipocalin family members. The non-native helix content in the burst-phase folding appears to depend on helical propensities of the amino acid sequence. |
| DOI | 10.1002/prot.22340 |
| ISSN | 0887-3585 |