{"created":"2023-06-20T16:46:12.573411+00:00","id":17646,"links":{},"metadata":{"_buckets":{"deposit":"7d698b34-c33f-44ad-a47b-727081113d76"},"_deposit":{"created_by":29,"id":"17646","owners":[29],"pid":{"revision_id":0,"type":"depid","value":"17646"},"status":"published"},"_oai":{"id":"oai:kindai.repo.nii.ac.jp:00017646","sets":["14:923:2219:4273"]},"author_link":["29825"],"item_2_biblio_info_21":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2016-05-31","bibliographicIssueDateType":"Issued"},"bibliographicPageEnd":"31","bibliographicPageStart":"23","bibliographicVolumeNumber":"21","bibliographic_titles":[{"bibliographic_title":"近畿大学先端技術総合研究所紀要"},{"bibliographic_title":"Memoirs of Institute of Advanced Technology, Kindai University","bibliographic_titleLang":"en"}]}]},"item_2_description_33":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"蛋白質の立体構造は一次元に連なったアミノ酸残基がアミノ酸配列に特有な3 次元構造に自発的にフォールディングして形成される。近年のゲノム配列決定の進展から数多くの蛋白質の遺伝子が解明されているが、アミノ酸配列のみから3 次元立体構造を決定することは、一部の小さな蛋白質を除き、未だに大変困難である。本研究では構造変性過程（アンフォールディング）を詳細に研究する試みから構造形成過程（フォールディング）の手がかりを得ることを目指して、20 残基のアミノ酸で構成されるミニ蛋白質であるTrp-cage 蛋白質の高熱及び高圧力による構造変性過程を、分子動力学シミュレーションで計算機上に再現して得られたデータを解析した。その結果、Trp-cage の変性は疎水性コアと2 次構造が協調して大きく揺らぐことで進行してゆくことが示唆される結果を得た。この結果は今後一般の蛋白質のフォールディング過程の研究に役立つと思われる。\nProteins spontaneously fold in living system, obeying thermodynamics principle. However, at present, it is not possible to provide the three-dimensional structure from the corresponding amino-acid sequence by only using theory and computation. Proteins are very complex matter in the world, involving huge degree of freedom. We have tackled the folding problem with respect to well-studied 20 residues mini-protein Trp-cage. We conducted three different long 0.5 μs molecular dynamics simulations, 1） 310 K and 1 atm, 2） 350 K and 1 atm, 3） 310 K and 2000 atm together with explicit water environment. As a result, it was observed that high-temperature increases the fluctuation of the system, in particular, the secondary structure, the accessible surface area and the radius of gyration of Trp-cage protein. In contrast, highpressure decreases the fluctuation significantly. These observation suggests that the secondary structure and hydrophobic core are fluctuating cooperatively. The results are useful for further study toward the general folding process of proteins.","subitem_description_type":"Abstract"}]},"item_2_description_41":{"attribute_name":"フォーマット","attribute_value_mlt":[{"subitem_description":"application/pdf","subitem_description_type":"Other"}]},"item_2_publisher_14":{"attribute_name":"出版者 名前","attribute_value_mlt":[{"subitem_publisher":"近畿大学先端技術総合研究所"}]},"item_2_source_id_22":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"13468693","subitem_source_identifier_type":"ISSN"}]},"item_2_text_7":{"attribute_name":"著者(英)","attribute_value_mlt":[{"subitem_text_language":"en","subitem_text_value":"Yonezawa, Yasushige"}]},"item_2_text_8":{"attribute_name":"著者 所属","attribute_value_mlt":[{"subitem_text_value":"近畿大学先端技術総合研究所高圧力蛋白質研究センター"}]},"item_2_text_9":{"attribute_name":"著者所属(翻訳)","attribute_value_mlt":[{"subitem_text_value":"Kindai University"}]},"item_2_version_type_12":{"attribute_name":"版","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_970fb48d4fbd8a85","subitem_version_type":"VoR"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"米澤, 康滋"},{"creatorName":"ヨネザワ, ヤスシゲ","creatorNameLang":"ja-Kana"}],"nameIdentifiers":[{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2016-08-02"}],"displaytype":"detail","filename":"AA11574630-20160531-0023.pdf","filesize":[{"value":"805.0 kB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"AA11574630-20160531-0023.pdf","url":"https://kindai.repo.nii.ac.jp/record/17646/files/AA11574630-20160531-0023.pdf"},"version_id":"1b579258-b3b0-47b9-8887-c39dca4fa260"}]},"item_keyword":{"attribute_name":"キーワード","attribute_value_mlt":[{"subitem_subject":"分子動力学シミュレーション","subitem_subject_scheme":"Other"},{"subitem_subject":"蛋白質フォールディング","subitem_subject_scheme":"Other"},{"subitem_subject":"熱変性","subitem_subject_scheme":"Other"},{"subitem_subject":"圧力変性","subitem_subject_scheme":"Other"},{"subitem_subject":"安定性","subitem_subject_scheme":"Other"},{"subitem_subject":"protein stability","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"folding","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"unfolding","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"molecular dynamics simulation","subitem_subject_language":"en","subitem_subject_scheme":"Other"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"jpn"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"departmental bulletin paper","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"〈Original Papers〉分子動力学シミュレーションによるTrp-cage蛋白質の高温及び高圧力環境下でのアンフォールディング過程研究","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"〈Original Papers〉分子動力学シミュレーションによるTrp-cage蛋白質の高温及び高圧力環境下でのアンフォールディング過程研究"},{"subitem_title":"Molecular Dynamics Simulation Study on the Unfolding Processes in Trp-cage protein under high-Pressure and high-Temperature","subitem_title_language":"en"}]},"item_type_id":"2","owner":"29","path":["4273"],"pubdate":{"attribute_name":"公開日","attribute_value":"2016-08-02"},"publish_date":"2016-08-02","publish_status":"0","recid":"17646","relation_version_is_last":true,"title":["〈Original Papers〉分子動力学シミュレーションによるTrp-cage蛋白質の高温及び高圧力環境下でのアンフォールディング過程研究"],"weko_creator_id":"29","weko_shared_id":-1},"updated":"2023-06-20T22:03:46.762112+00:00"}