De Novo Proteins with Life-Sustaining Functions Are Structurally Dynamic

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• 作者：Grant S. Murphy ; Jack B. Greisman¹ ; Michael H. Hecht ; ^{hecht@princeton.edu" class="auth_mail" title="E-mail the corresponding author}
• 关键词：NOE ; Nuclear Overhauser effect ; HSQC ; heteronuclear single quantum coherence ; SEC ; size-exclusion chromatography ; IMAC ; immobilized metal affinity chromatography
• 刊名：Journal of Molecular Biology
• 出版年：2016
• 出版时间：29 January 2016
• 年：2016
• 卷：428
• 期：2
• 页码：399-411
• 全文大小：1232 K

文摘

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d="p0340">Well-ordered protein structure is commonly assumed to be an essential feature of protein function.

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d="p0345">Here we investigated the biophysical and structural properties of a family of de novo designed proteins that provide life-sustaining functions in E. coli.

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d="p0350">We discovered that the de novo proteins tested here do not form well-ordered structures and instead form dynamic dimer structures.

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d="p0355">These results highlight the importance of protein dynamics in protein function and also suggest that dynamic structures may have been important in early evolution.

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