Literature DB >> 24466578

Membrane proteins by accident or design.

John Simms, Paula J Booth.   

Abstract

Protein design is a valuable tool to create bespoke proteins with desired properties as well as for investigating sequence, structure and function relationships. Membrane protein design is a burgeoning field that is hampered by the lack of high-resolution structural information. In spite of these shortcomings, computational methods have offered a route towards blueprints for these hydrophobic proteins. Advances in structural scoring and sampling methods are enabling more accurate predictions of a folded structure from the primary amino acid sequence. This review highlights a number of novel studies focusing on the methods and information used to successfully design membrane proteins.

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Year:  2013        PMID: 24466578     DOI: 10.1016/j.cbpa.2013.10.005

Source DB:  PubMed          Journal:  Curr Opin Chem Biol        ISSN: 1367-5931            Impact factor:   8.822


  3 in total

Review 1.  Membrane-spanning α-helical barrels as tractable protein-design targets.

Authors:  Ai Niitsu; Jack W Heal; Kerstin Fauland; Andrew R Thomson; Derek N Woolfson
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2017-08-05       Impact factor: 6.237

Review 2.  Outer membrane protein design.

Authors:  Joanna Sg Slusky
Journal:  Curr Opin Struct Biol       Date:  2016-11-26       Impact factor: 6.809

Review 3.  Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.

Authors:  Andrew Currin; Neil Swainston; Philip J Day; Douglas B Kell
Journal:  Chem Soc Rev       Date:  2015-03-07       Impact factor: 54.564

  3 in total

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