Enhancing RGI lyase thermostability by targeted single point mutations-Reference-Cited by-同舟云学术

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Enhancing RGI lyase thermostability by targeted single point mutations

Published:2013-08-31 Issue:22 Volume:97 Page:9727-9735
ISSN:0175-7598
Container-title:Applied Microbiology and Biotechnology
language:en
Short-container-title:Appl Microbiol Biotechnol

Author:

Silva Inês R.,Larsen Dorte M.,Jers Carsten,Derkx Patrick,Meyer Anne S.,Mikkelsen Jørn D.

Publisher

Springer Science and Business Media LLC

Subject

Applied Microbiology and Biotechnology,General Medicine,Biotechnology

Link

http://link.springer.com/content/pdf/10.1007/s00253-013-5184-3.pdf

Reference45 articles.

1. Bommarius AS, Broering JM, Chaparro-Riggers JF, Polizzi KM (2006) High-throughput screening for enhanced protein stability. Curr Opin Biotechnol 17:606–610

2. Cole MF, Gaucher EA (2011) Utilizing natural diversity to evolve protein function: applications towards thermostability. Curr Opin Chem Biol 15:399–406

3. Dalby PA (2011) Strategy and success for the directed evolution of enzymes. Curr Opin Struct Biol 21:473–480

4. Davidson AR (2006) Multiple sequence alignment as a guideline for protein engineering strategies. Methods Mol Biol 340:171–181

5. Dehouck Y, Grosfils A, Folch B, Gilis D, Bogaerts P, Rooman M (2009) Fast and accurate predictions of protein stability changes upon mutations using statistical potentials and neural networks: PoPMuSiC-2.0. Bioinformatics 25:2537–2543

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