{"created":"2023-06-20T13:23:27.633294+00:00","id":4316,"links":{},"metadata":{"_buckets":{"deposit":"ca08123f-a670-464a-aeba-f258c39eb0f5"},"_deposit":{"created_by":21,"id":"4316","owners":[21],"pid":{"revision_id":0,"type":"depid","value":"4316"},"status":"published"},"_oai":{"id":"oai:ir.soken.ac.jp:00004316","sets":["1:323"]},"author_link":["2361","2520","2364","3119"],"item_10001_biblio_info_7":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2004-08-06","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"2","bibliographicPageEnd":"604","bibliographicPageStart":"589","bibliographicVolumeNumber":"341","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":"To investigate whether the structure partially formed in the molten globule folding intermediate of goat α-lactalbumin is further organized in the transition state of folding, we constructed a number of mutant proteins and performed Φ-value analysis on them. For this purpose, we measured the equilibrium unfolding transitions and kinetic refolding and unfolding reactions of the mutants using equilibrium and stopped-flow kinetic circular dichroism techniques. The results show that the mutants with mutations located in the A-helix (V8A, L12A), the B-helix (V27A), the β-domain (L52A, W60A), the C-helix (K93A, L96A), the C–D loop (Y103F), the D-helix (L105A, L110A), and the C-terminal 310-helix (W118F), have low Φ-values, less than 0.2. On the other hand, D87N, which is located on the Ca2+-binding site, has a high Φ-value, 0.91, indicating that tight packing of the side-chain around Asp87 occurs in the transition state. One β-domain mutant (I55V) and three C-helix mutants (I89V, V90A, and I95V) demonstrated intermediate Φ-values, between 0.4 and 0.7. These results indicate that the folding nucleus in the transition state of goat α-LA is not extensively distributed over the α-domain of the protein, but very localized in a region that contains the Ca2+-binding site and the interface between the C-helix and the β-domain. This is apparently in contrast with the fact that the molten globule state of α-lactalbumin has a partially formed structure inside the α-domain. It is concluded that the specific docking of the α and β-domains at a domain interface is necessary for this protein to organize its native structure from the molten globule intermediate.","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.2004.06.010"}],"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://doi.org/10.1016/j.jmb.2004.06.010","subitem_relation_type_select":"DOI"}}]},"item_10001_rights_15":{"attribute_name":"権利","attribute_value_mlt":[{"subitem_rights":"© 2004 Elsevier Ltd."}]},"item_10001_source_id_26":{"attribute_name":"Online 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":"SAEKI, Kimiko"}],"nameIdentifiers":[{"nameIdentifier":"2520","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":"Localized Nature of the Transition-state Structure in Goat α-Lactalbumin Folding","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Localized Nature of the Transition-state Structure in Goat α-Lactalbumin Folding"},{"subitem_title":"Localized Nature of the Transition-state Structure in Goat α-Lactalbumin Folding","subitem_title_language":"en"}]},"item_type_id":"10001","owner":"21","path":["323"],"pubdate":{"attribute_name":"公開日","attribute_value":"2014-03-19"},"publish_date":"2014-03-19","publish_status":"0","recid":"4316","relation_version_is_last":true,"title":["Localized Nature of the Transition-state Structure in Goat α-Lactalbumin Folding"],"weko_creator_id":"21","weko_shared_id":21},"updated":"2023-06-20T14:24:02.930913+00:00"}