Literature DB >> 11551465

Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution.

M Lehmann1, M Wyss.   

Abstract

With the advent of directed evolution techniques, protein engineering has received a fresh impetus. Engineering proteins for thermostability is a particularly exciting and challenging field, as it is crucial for broadening the industrial use of recombinant proteins. In addition to directed evolution, a variety of partially successful rational concepts for engineering thermostability have been developed in the past. Recent results suggest that amino acid sequence comparisons of mesophilic proteins alone can be used efficiently to engineer thermostable proteins. The potential benefits of the underlying, semirational 'consensus concept' are compared with those of rational design and directed evolution approaches.

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Year:  2001        PMID： 11551465     DOI： 10.1016/s0958-1669(00)00229-9

Source DB:  PubMed          Journal:  Curr Opin Biotechnol        ISSN： 0958-1669            Impact factor:   9.740


  69 in total

1.  Directed evolution of mammalian anti-apoptosis proteins by somatic hypermutation.

Authors:  Brian S Majors; Gisela G Chiang; Nels E Pederson; Michael J Betenbaugh
Journal:  Protein Eng Des Sel       Date:  2011-12-09       Impact factor: 1.650

2.  Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability.

Authors:  Mats Sandgren; Peter J Gualfetti; Andrew Shaw; Laurie S Gross; Mae Saldajeno; Anthony G Day; T Alwyn Jones; Colin Mitchinson
Journal:  Protein Sci       Date:  2003-04       Impact factor: 6.725

3.  Introduction of a disulfide bridge enhances the thermostability of a Streptomyces olivaceoviridis xylanase mutant.

Authors:  H M Yang; B Yao; K Meng; Y R Wang; Y G Bai; N F Wu
Journal:  J Ind Microbiol Biotechnol       Date:  2006-12-01       Impact factor: 3.346

4.  Thermostabilizing mutations in reovirus outer-capsid protein mu1 selected by heat inactivation of infectious subvirion particles.

Authors:  Jason K Middleton; Melina A Agosto; Tonya F Severson; John Yin; Max L Nibert
Journal:  Virology       Date:  2007-01-17       Impact factor: 3.616

5.  Bioinformatic method for protein thermal stabilization by structural entropy optimization.

Authors:  Euiyoung Bae; Ryan M Bannen; George N Phillips
Journal:  Proc Natl Acad Sci U S A       Date:  2008-07-08       Impact factor: 11.205

6.  Insertion of endocellulase catalytic domains into thermostable consensus ankyrin scaffolds: effects on stability and cellulolytic activity.

Authors:  Eva S Cunha; Christine L Hatem; Doug Barrick
Journal:  Appl Environ Microbiol       Date:  2013-08-23       Impact factor: 4.792

7.  Probing impact of active site residue mutations on stability and activity of Neisseria polysaccharea amylosucrase.

Authors:  David Daudé; Christopher M Topham; Magali Remaud-Siméon; Isabelle André
Journal:  Protein Sci       Date:  2013-10-21       Impact factor: 6.725

8.  Combinatorial engineering to enhance thermostability of amylosucrase.

Authors:  Stéphane Emond; Isabelle André; Kais Jaziri; Gabrielle Potocki-Véronèse; Philippe Mondon; Khalil Bouayadi; Hakim Kharrat; Pierre Monsan; Magali Remaud-Simeon
Journal:  Protein Sci       Date:  2008-04-25       Impact factor: 6.725

9.  Increasing protein conformational stability by optimizing beta-turn sequence.

Authors:  Saul R Trevino; Stephanie Schaefer; J Martin Scholtz; C Nick Pace
Journal:  J Mol Biol       Date:  2007-08-09       Impact factor: 5.469

10.  Thermostable variants of cocaine esterase for long-time protection against cocaine toxicity.

Authors:  Daquan Gao; Diwahar L Narasimhan; Joanne Macdonald; Remy Brim; Mei-Chuan Ko; Donald W Landry; James H Woods; Roger K Sunahara; Chang-Guo Zhan
Journal:  Mol Pharmacol       Date:  2008-11-05       Impact factor: 4.436
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