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Experimental studies of folding kinetics and structural dynamics of small proteins
https://ir.soken.ac.jp/records/4128
https://ir.soken.ac.jp/records/412843315d0d-869f-4cb0-9b58-a8a90dc412d1
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2013-12-25 | |||||
| タイトル | ||||||
| タイトル | Experimental studies of folding kinetics and structural dynamics of small proteins | |||||
| タイトル | ||||||
| タイトル | Experimental studies of folding kinetics and structural dynamics of small proteins | |||||
| 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 |
KUWAJIMA, Kunihiro
× KUWAJIMA, Kunihiro× SCHMID, Franz X |
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| 著者別名 |
桑島, 邦博
× 桑島, 邦博 |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Main points given in the above reports can be summarized as follows. 1.(1) Multiple unfolded forms exists for lysozyme as well as for RNase. The existence of fast- and slow-folding forms appears to be a general phenomenon; it has been confirmed for a number of globular proteins, which contain proline residues (5,35,43,95–98). 2.(2) The major slow refolding reaction of RNase A is a sequential process via structural intermediates. A rapidly formed intermediate has also been detected on the direct UY → N refolding pathways of lysozyme. 3.(3) The activated state for folding of lysozyme shows a conformation similar to the native protein in terms of packing of hydrophobic groups. This suggests that, in tersm of compactness, the rate-limitin step occurs at a late stage of the refolding process. A protein homologous to lysozyme, α-lactalbumin, shows similar kinetics although α-lactalbumin shows an apparent equilibrium unfolding intermediate (99, 100). The location of the rate-limiting step close to the native state has also been suggested for other proteins (6, 101–103). It still remains open whether this is a general property of protein folding reactions. 4.(4) As shown for the unfolding of Mb, the multi-probe kinetic measurements will be a powerful tool for investigating the mechanism of folding, in particular for characterizing structural kinetic intermediates. 5.(5) The dynamics of local fluctuations of a well-defined part of RNase S can be monitored by NMR measurements of NH proton exchange. An increasing number of experimental (1,10,79) and the theoretical (11) studies are focusing on the problem of protein dynamics. Application of NMR methods to protein folding should give extensive information about the structure of intermerdiates, which cannot be given by other techniquees. |
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| 書誌情報 |
Advances in Biophysics en : Advances in Biophysics 巻 18, p. 43-74, 発行日 1984 |
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| 出版者 | ||||||
| 出版者 | Elsevier | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0065227X | |||||
| PubMed番号 | ||||||
| 識別子タイプ | PMID | |||||
| 関連識別子 | 6399821 | |||||
| 権利 | ||||||
| 権利情報 | © 1984 Published by Elsevier Ireland Ltd. | |||||
| 関連サイト | ||||||
| 識別子タイプ | URI | |||||
| 関連識別子 | http://www.sciencedirect.com/science/article/pii/0065227X84900066 | |||||
| 関連名称 | Elsevier | |||||
