Engineering Protein Sequence Composition for Folding Robustness Renders Efficient Noncanonical Amino acid Incorporations

被引：30

作者：

Nagasundarapandian, Soundrarajan ^{[1
]}

Merkel, Lars ^{[2
]}

Budisa, Nediljko ^{[2
]}

Govindan, Raghunathan ^{[1
]}

Ayyadurai, Niraikulam ^{[3
]}

Sriram, Sokalingam ^{[1
]}

Yun, Hyungdon ^{[3
]}

Lee, Sun-Gu ^{[1
]}

机构：

[1] Pusan Natl Univ, Dept Chem Engn, Pusan 609735, South Korea

[2] Tech Univ Berlin, Dept Chem, Biocatalysis Grp, D-10587 Berlin, Germany

[3] Yeungnam Univ, Sch Biotechnol, Gyongsan 712749, South Korea

来源：

CHEMBIOCHEM | 2010年 / 11卷 / 18期

关键词：

amino acids; methionine; mutations; noncanonical amino acids; protein engineering; GREEN FLUORESCENT PROTEIN; GENETIC-CODE; REPERTOIRE; BACTERIAL; EVOLUTION; CELLS; GFP;

D O I：

10.1002/cbic.201000380

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Folding up: Residue-specific incorporation of noncanonical amino acids (NCAAs) often results in loss of protein function either by misfolding or aggregation (left). However, engineering the protein sequence for enhanced folding increases the mutational robustness of the protein to accommodate novel side chains and generate tailor-made proteins with new properties (right). © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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收藏

页码：2521 / 2524

页数：4

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