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| Title Transcription | タンパクシツ ノ フォールディング オ ホジョ スル シャペロニン ノ コウゾウ ト ハタラキ
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| Title Alternative | Structure and function of chaperonins, molecular assistants of protein folding
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| Authors | |
| Keywords | Protein folding
Stress response
Molecular chaperones
Chaperonins
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| Abstract | Proteins in the cell are routinely exposed to various conditions that promote unfolding and irreversible aggregation. Chaperonins act to prevent protein denaturation and aggregation by sequestering aggregation-prone protein molecules and encouraging recovery. Chaperonin function is supported by various static and dynamic characteristics of its unique structure. This article summarizes some of our results regarding the structural characteristics that support the function of the Escherichia coli chaperonin GroE.
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| Publisher | 鳥取大学大学院工学研究科
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| Content Type |
Departmental Bulletin Paper
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| ISSN | 0385-8596
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| Journal Title | 鳥取大学大学院工学研究科／工学部研究報告
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| Current Journal Title |
Reports of the Faculty of Engineering, Tottori University
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| Volume | 41
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| Start Page | 29
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| End Page | 35
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| Published Date | 2010-12-24
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| Text Version |
Publisher
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| Citation | 鳥取大学大学院工学研究科／工学部研究報告. 2010, 41, 29-35
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| Department |
Faculty of Engineering/Graduate School of Engineering
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| Language |
Japanese
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