| Item type |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2014-03-12 |
| タイトル |
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タイトル |
Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy |
| タイトル |
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タイトル |
Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy |
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言語 |
en |
| 言語 |
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言語 |
eng |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| アクセス権 |
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アクセス権 |
metadata only access |
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アクセス権URI |
http://purl.org/coar/access_right/c_14cb |
| 著者 |
ARAI, Munehito
IKURA, Teikichi
SEMISOTNOV, Gennady V
KIHARA, Hiroshi
AMEMIYA, Yoshiyuki
KUWAJIMA, Kunihiro
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| 著者別名 |
桑島, 邦博
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| 抄録 |
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内容記述タイプ |
Abstract |
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内容記述 |
β-Lactoglobulin (βLG) is a predominantly β-sheet protein with a markedly high helical propensity and forms non-native α-helical intermediate in the refolding process. We measured the refolding reaction of βLG with various techniques and characterized the folding kinetics and the structure of the intermediate formed within the burst phase of measurements, i.e. the burst-phase intermediate. Time-resolved stopped-flow X-ray scattering measurements using the integral intensity of scattering show that βLG forms a compact, globular structure within 30 ms of refolding. The averaged radius of gyration within 100 ms is only 1.1 times larger than that in the native state, ensuring that the burst-phase intermediate is compact. The presence of a maximum peak in a Kratky plot shows a globular shape attained within 100 ms of refolding. Stopped-flow circular dichroism, tryptophan absorption and fluorescence spectroscopy show that pronounced secondary structure regains rapidly in the burst phase with concurrent non-native α-helix formation, and that the subsequent compaction process is accompanied by annealing of non-native secondary structure and slow acquisition of tertiary structure. These findings strongly suggest that both compaction and secondary structure formation in protein folding are quite rapid processes, taking place within a millisecond time-scale. The structure of the burst-phase intermediate in βLG refolding was characterized as having a compact size, a globular shape, a hydrophobic core, substantial β-sheets and remarkable non-native α-helical structure, but little tertiary structure. These results suggest that both local interactions and non-local hydrophobic interactions are dominant forces early in protein folding. The interplay of local and non-local interactions throughout folding processes is important in understanding the mechanisms of protein folding. |
| 書誌情報 |
Journal of Molecular Biology
en : Journal of Molecular Biology
巻 275,
号 1,
p. 149-162,
発行日 1998-01-09
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| 出版者 |
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出版者 |
Elsevier |
| ISSN |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
0022-2836 |
| DOI |
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識別子タイプ |
DOI |
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関連識別子 |
https://doi.org/10.1006/jmbi.1997.1456 |
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関連名称 |
10.1006/jmbi.1997.1456 |
| 権利 |
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権利情報 |
© 1998 Academic Press |
