The role of proline substitutions within flexible regions on thermostability of luciferase-Reference-Cited by-同舟云学术

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The role of proline substitutions within flexible regions on thermostability of luciferase

Published:2015-01 Issue:1 Volume:1854 Page:65-72
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Yu Haoran,Zhao Yang,Guo Chao,Gan Yiru,Huang He

Funder

National High-tech R&D program

National Natural Science Foundation of China

National Science and Technology Major Projects of China

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference46 articles.

1. Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions;Inouye;Cell. Mol. Life Sci.,2010

2. Design and characterization of novel trypsin-resistant firefly luciferases by site-directed mutagenesis;Riahi-Madvar;Protein Eng. Des. Sel.,2009

3. Approaches to engineer stability of beetle luciferases;Koksharov;Comput. Struct. Biotechnol. J.,2012

4. Mutagenesis of solvent-exposed amino acids in Photinus pyralis luciferase improves thermostability and pH-tolerance;Law;Biochem. J.,2006

5. Design and introduction of a disulfide bridge in firefly luciferase: increase of thermostability and decrease of pH sensitivity;Imani;Photochem. Photobiol. Sci.,2010

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