WEKO3
アイテム
Folding-unfolding of goat α-lactalbumin studied by stopped-flow circular dichroism and molecular dynamics simulations
https://ir.soken.ac.jp/records/4301
https://ir.soken.ac.jp/records/4301ded96ee7-3f64-42ab-8ab6-a922ea5b3252
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2014-03-14 | |||||
| タイトル | ||||||
| タイトル | Folding-unfolding of goat α-lactalbumin studied by stopped-flow circular dichroism and molecular dynamics simulations | |||||
| タイトル | ||||||
| タイトル | Folding-unfolding of goat α-lactalbumin studied by stopped-flow circular dichroism and molecular dynamics simulations | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | journal article | |||||
| アクセス権 | ||||||
| アクセス権 | metadata only access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
| 著者 |
YODA, Takao
× YODA, Takao× KUWAJIMA, Kunihiro× et, al. |
|||||
| 著者別名 |
桑島, 邦博
× 桑島, 邦博 |
|||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Folding reaction of goat α-lactalbumin has been studied by stopped-flow circular dichroism and molecular dynamics simulations. The effects of four single mutations and a double mutation on the stability of the protein under a native condition were studied. The mutations were introduced into residues located at a hydrophobic core in the α-domain of the molecule. Here we show that an amino acid substitution (T29I) increases the native-state stability of goat α-lactalbumin against the guanidine hydrochloride-induced unfolding by 3.5 kcal/mol. Kinetic refolding and unfolding of wild-type and mutant goat α-lactalbumin measured by stopped-flow circular dichroism showed that the local structure around the Thr29 side chain was not constructed in the transition state of the folding reaction. To characterize the local structural change around the Thr29 side chain to an atomic level of resolution, we performed high-temperature (at 400 K and 600 K) molecular dynamics simulations and studied the structural change at an initial stage of unfolding observed in the simulation trajectories. The Thr29 portion of the molecule experienced structural disruption accompanied with the loss of inter-residue contacts and with the water molecule penetration in the 400-K simulation as well as in four of the six 600-K simulations. Disruption of the N-terminal portion was also observed and was consistent with the results of kinetic refolding/unfolding experiments shown in our previous report. | |||||
| 書誌情報 |
Proteins: Structure, Function, and Bioinformatics en : Proteins: Structure, Function, and Bioinformatics 巻 42, 号 1, p. 49-65, 発行日 2001-01-01 |
|||||
| 出版者 | ||||||
| 出版者 | Wiley | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0887-3585 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | https://doi.org/10.1002/1097-0134(20010101)42:1<49::AID-PROT60>3.0.CO;2-Z | |||||
| 関連名称 | 10.1002/1097-0134(20010101)42:1<49::AID-PROT60>3.0.CO;2-Z | |||||
| 権利 | ||||||
| 権利情報 | © 2000 Wiley-Liss, Inc. | |||||
