ログイン
言語:

WEKO3

  • トップ
  • ランキング
To
lat lon distance
To

Field does not validate



インデックスリンク

インデックスツリー

メールアドレスを入力してください。

WEKO

One fine body…

WEKO

One fine body…

アイテム

{"_buckets": {"deposit": "318bff9a-f204-4c9b-a166-08d60400a651"}, "_deposit": {"created_by": 21, "id": "4329", "owners": [21], "pid": {"revision_id": 0, "type": "depid", "value": "4329"}, "status": "published"}, "_oai": {"id": "oai:ir.soken.ac.jp:00004329", "sets": ["323"]}, "author_link": ["2361", "2522", "2364", "3119"], "item_10001_biblio_info_7": {"attribute_name": "書誌情報", "attribute_value_mlt": [{"bibliographicIssueDates": {"bibliographicIssueDate": "2006-09-01", "bibliographicIssueDateType": "Issued"}, "bibliographicIssueNumber": "5", "bibliographicPageEnd": "982", "bibliographicPageStart": "969", "bibliographicVolumeNumber": "361", "bibliographic_titles": [{"bibliographic_title": "Journal of Molecular Biology"}, {"bibliographic_title": "Journal of Molecular Biology", "bibliographic_titleLang": "en"}]}]}, "item_10001_creator_3": {"attribute_name": "著者別名", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "桑島, 邦博"}], "nameIdentifiers": [{"nameIdentifier": "2364", "nameIdentifierScheme": "WEKO"}, {"nameIdentifier": "1000070091444", "nameIdentifierScheme": "NRID", "nameIdentifierURI": " "}, {"nameIdentifier": "70091444", "nameIdentifierScheme": "e-Rad", "nameIdentifierURI": "https://kaken.nii.ac.jp/ja/search/?qm=70091444"}]}]}, "item_10001_description_5": {"attribute_name": "抄録", "attribute_value_mlt": [{"subitem_description": "Folding mechanisms of a variant of green fluorescent protein (F99S/M153T/V163A) were investigated by a wide variety of spectroscopic techniques. Equilibrium measurements on acid-induced denaturation of the protein monitored by chromophore and tryptophan fluorescence and small-angle X-ray scattering revealed that this protein accumulates at least two equilibrium intermediates, a native-like intermediate and an unfolding intermediate, the latter of which exhibits the characteristics of the molten globule state under moderately denaturing conditions at pH 4. To elucidate the role of the equilibrium unfolding intermediate in folding, a series of kinetic refolding experiments with various combinations of initial and final pH values, including pH 7.5 (the native condition), pH 4.0 (the moderately denaturing condition where the unfolding intermediate is accumulated), and pH 2.0 (the acid-denaturing condition) were carried out by monitoring chromophore and tryptophan fluorescence. Kinetic on-pathway intermediates were accumulated during the folding on the refolding reaction from pH 2.0 to 7.5. However, the signal change corresponding to the conversion from the acid-denatured to the kinetic intermediate states was significantly reduced on the refolding reaction from pH 4.0 to pH 7.5, whereas only the signal change corresponding to the above conversion was observed on the refolding reaction from pH 2.0 to pH 4.0. These results indicate that the equilibrium unfolding intermediate is composed of an ensemble of the folding intermediate species accumulated during the folding reaction, and thus support a hierarchical model of protein folding.", "subitem_description_type": "Abstract"}]}, "item_10001_publisher_8": {"attribute_name": "出版者", "attribute_value_mlt": [{"subitem_publisher": "Elsevier "}]}, "item_10001_relation_14": {"attribute_name": "DOI", "attribute_value_mlt": [{"subitem_relation_name": [{"subitem_relation_name_text": "10.1016/j.jmb.2006.07.009"}], "subitem_relation_type_id": {"subitem_relation_type_id_text": "https://doi.org/10.1016/j.jmb.2006.07.009", "subitem_relation_type_select": "DOI"}}]}, "item_10001_rights_15": {"attribute_name": "権利", "attribute_value_mlt": [{"subitem_rights": "© 2006 Elsevier Ltd. "}]}, "item_10001_source_id_9": {"attribute_name": "ISSN", "attribute_value_mlt": [{"subitem_source_identifier": "0022-2836 ", "subitem_source_identifier_type": "ISSN"}]}, "item_access_right": {"attribute_name": "アクセス権", "attribute_value_mlt": [{"subitem_access_right": "metadata only access", "subitem_access_right_uri": "http://purl.org/coar/access_right/c_14cb"}]}, "item_creator": {"attribute_name": "著者", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "ENOKI, Sawako"}], "nameIdentifiers": [{"nameIdentifier": "2522", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "KUWAJIMA, Kunihiro "}], "nameIdentifiers": [{"nameIdentifier": "2361", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "et, al."}], "nameIdentifiers": [{"nameIdentifier": "3119", "nameIdentifierScheme": "WEKO"}]}]}, "item_language": {"attribute_name": "言語", "attribute_value_mlt": [{"subitem_language": "eng"}]}, "item_resource_type": {"attribute_name": "資源タイプ", "attribute_value_mlt": [{"resourcetype": "journal article", "resourceuri": "http://purl.org/coar/resource_type/c_6501"}]}, "item_title": "The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein", "item_titles": {"attribute_name": "タイトル", "attribute_value_mlt": [{"subitem_title": "The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein"}, {"subitem_title": "The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein", "subitem_title_language": "en"}]}, "item_type_id": "10001", "owner": "21", "path": ["323"], "permalink_uri": "https://ir.soken.ac.jp/records/4329", "pubdate": {"attribute_name": "公開日", "attribute_value": "2014-03-25"}, "publish_date": "2014-03-25", "publish_status": "0", "recid": "4329", "relation": {}, "relation_version_is_last": true, "title": ["The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein"], "weko_shared_id": 21}
  1. 010 学術雑誌論文
  2. 桑島, 邦博 / KUWAJIMA, Kunihiro

The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein

https://ir.soken.ac.jp/records/4329
https://ir.soken.ac.jp/records/4329
5ff789c7-9ad2-4323-857a-47598200e706
Item type 学術雑誌論文 / Journal Article(1)
公開日 2014-03-25
タイトル
タイトル The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein
タイトル
言語 en
タイトル The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein
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 ENOKI, Sawako

× ENOKI, Sawako

WEKO 2522

ENOKI, Sawako

Search repository
KUWAJIMA, Kunihiro

× KUWAJIMA, Kunihiro

WEKO 2361

KUWAJIMA, Kunihiro

Search repository
et, al.

× et, al.

WEKO 3119

et, al.

Search repository
著者別名 桑島, 邦博

× 桑島, 邦博

WEKO 2364
NRID 1000070091444
e-Rad 70091444

桑島, 邦博

Search repository
抄録
内容記述タイプ Abstract
内容記述 Folding mechanisms of a variant of green fluorescent protein (F99S/M153T/V163A) were investigated by a wide variety of spectroscopic techniques. Equilibrium measurements on acid-induced denaturation of the protein monitored by chromophore and tryptophan fluorescence and small-angle X-ray scattering revealed that this protein accumulates at least two equilibrium intermediates, a native-like intermediate and an unfolding intermediate, the latter of which exhibits the characteristics of the molten globule state under moderately denaturing conditions at pH 4. To elucidate the role of the equilibrium unfolding intermediate in folding, a series of kinetic refolding experiments with various combinations of initial and final pH values, including pH 7.5 (the native condition), pH 4.0 (the moderately denaturing condition where the unfolding intermediate is accumulated), and pH 2.0 (the acid-denaturing condition) were carried out by monitoring chromophore and tryptophan fluorescence. Kinetic on-pathway intermediates were accumulated during the folding on the refolding reaction from pH 2.0 to 7.5. However, the signal change corresponding to the conversion from the acid-denatured to the kinetic intermediate states was significantly reduced on the refolding reaction from pH 4.0 to pH 7.5, whereas only the signal change corresponding to the above conversion was observed on the refolding reaction from pH 2.0 to pH 4.0. These results indicate that the equilibrium unfolding intermediate is composed of an ensemble of the folding intermediate species accumulated during the folding reaction, and thus support a hierarchical model of protein folding.
書誌情報 Journal of Molecular Biology
en : Journal of Molecular Biology

巻 361, 号 5, p. 969-982, 発行日 2006-09-01
出版者
出版者 Elsevier
ISSN
収録物識別子タイプ ISSN
収録物識別子 0022-2836
DOI
識別子タイプ DOI
関連識別子 https://doi.org/10.1016/j.jmb.2006.07.009
関連名称 10.1016/j.jmb.2006.07.009
権利
権利情報 © 2006 Elsevier Ltd.
戻る
0
views
See details
Views

Versions

Ver.1 2023-06-20 14:24:56.137348
Show All versions

Share

Mendeley Twitter Facebook Print Addthis

Cite as

エクスポート

OAI-PMH
  • OAI-PMH JPCOAR
  • OAI-PMH DublinCore
  • OAI-PMH DDI
Other Formats
  • JSON
  • BIBTEX

Confirm


Powered by WEKO3


Powered by WEKO3