{"created":"2023-05-15T14:33:51.770274+00:00","id":43927,"links":{},"metadata":{"_buckets":{"deposit":"901a8f81-3982-4fa1-b0f1-c09868e75f5c"},"_deposit":{"created_by":1,"id":"43927","owners":[1],"pid":{"revision_id":0,"type":"depid","value":"43927"},"status":"published"},"_oai":{"id":"oai:repo.qst.go.jp:00043927","sets":["1"]},"author_link":["436703","436701","436704","436706","436702","436705"],"item_8_biblio_info_7":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"1997-10","bibliographicIssueDateType":"Issued"},"bibliographicPageEnd":"716","bibliographicPageStart":"711","bibliographicVolumeNumber":"122","bibliographic_titles":[{"bibliographic_title":"Journal of Biochemistry"}]}]},"item_8_description_5":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"Max is a basic region/helix-loop-helix/leucine zipper (b/HLH/Z) protein that forms a hetero-complex with the Myc family proteins Myc, Mad, and Mxi1, and a homo-complex with itself. These complexes specifically bind to double-stranded DNA containing CACGTG sequences. Here, we report on the structural properties in aqueous solution of a 109-amino-acid protein, Max110, corresponding to the N-terminal domain of Max containing the b/HLH/Z motif (residues 2-110), as characterized by combined use of circular dichroism (CD) and sedimentation equilibrium experiments. The results showed that the alpha-helical content of Max110 increases with increasing protein concentration. The sedimentation equilibrium data indicated that Max110 exists as a monomer at low protein concentration, and forms a dimer at high protein concentration. Further increases in the alpha-helical content of Max110 occur upon addition of DNA with the CACGTG recognition sequence. Thus, dimerization and binding to DNA of Max both favor an increase of the alpha-helical content.","subitem_description_type":"Abstract"}]},"item_8_source_id_9":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"0021-924X","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":"Kurihara, Yasuyuki"}],"nameIdentifiers":[{"nameIdentifier":"436701","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Katahira, Masato"}],"nameIdentifiers":[{"nameIdentifier":"436702","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Saito, Toshiyuki"}],"nameIdentifiers":[{"nameIdentifier":"436703","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Uesugi, Seiichi"}],"nameIdentifiers":[{"nameIdentifier":"436704","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"et.al"}],"nameIdentifiers":[{"nameIdentifier":"436705","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"齋藤 俊行","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"436706","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":"Dimerization and DNA binding facilitate alpha-helix formation of Max in solution.","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Dimerization and DNA binding facilitate alpha-helix formation of Max in solution."}]},"item_type_id":"8","owner":"1","path":["1"],"pubdate":{"attribute_name":"公開日","attribute_value":"2005-12-16"},"publish_date":"2005-12-16","publish_status":"0","recid":"43927","relation_version_is_last":true,"title":["Dimerization and DNA binding facilitate alpha-helix formation of Max in solution."],"weko_creator_id":"1","weko_shared_id":-1},"updated":"2023-05-16T00:21:26.382961+00:00"}