Cited by 215Protein Structure and DynamicsProtein purification and stabilityEnzyme Catalysis and Immobilization

Consensus protein design

Open access
Porebski, Benjamin T., Buckle, Ashley M.·2016·Protein Engineering Design and Selection

Abstract

A popular and successful strategy in semi-rational design of protein stability is the use of evolutionary information encapsulated in homologous protein sequences. Consensus design is based on the hypothesis that at a given position, the respective consensus amino acid contributes more than average to the stability of the protein than non-conserved amino acids. Here, we review the consensus design approach, its theoretical underpinnings, successes, limitations and challenges, as well as providing a detailed guide to its application in protein engineering.

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Crossref · 10.1093/protein/gzw015

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  • Consensus sequences determined by multiple sequence alignment are believed to play a crucial part in maintaining protein stability and adhesion throughout evolution.

    “We then performed multiple sequence alignment using Clustal Omega23 to determine consensus sequences for each species (Extended Data Fig. 1), which are believed to play a crucial part in maintaining protein stability and adhesion throughout evolution24,25.”

    From Data-driven de novo design of super-adhesive hydrogels (2025) · cites this paper as [24]

    The Introduction describes deriving consensus sequences from multiple sequence alignments, and ‘Engineering thermodynamic stability’ explains why conserved residues are more likely to stabilize proteins. Our copy does not support the attributed role in adhesion; it also notes that some conserved residues are neutral or destabilizing. (LLM, conf=0.88)

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Research works printed but not linked: 2

  1. Alton K., Stabinsky Y., Richards R., Ferguson B., Goldstein L., Altrock B., Miller L., Stebbing N. (1983) The Biology of Interferon System. 2nd ed. Amsterdam: Elsevier Science Publishers, pp. 119– 128.
  2. Pearson W.R. (2013) Curr Protoc Bioinformatics, 42, 3.1:3.1.1–3.1.8.

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Authors
Porebski, B. T., & Buckle, A. M.
Affiliations
  • MRC Laboratory of Molecular Biology (GB)
  • Monash University (AU)
Corresponding author
Buckle, Ashley M.
Venue
Protein Engineering Design and Selection
Published
2016-06-05
Volume
29
Issue
7
Pages
245-251
ISSN
  • 0269-2139 (ISSN-L)
  • 1741-0126
  • 1741-0134
OpenAlex
W2412714128
Cited by
215
References
110
Citations by year
2026: 21 · 2025: 25 · 2024: 26 · 2023: 25 · 2022: 29 · 2021: 27 · 2020: 16 · 2019: 16 · 2018: 15 · 2017: 10 · 2016: 5
FWCI
1.42
Type
journal article
Language
en
Open access
Licence
cc-by-nc
Locations
  • Protein Engineering Design and Selection (publishedVersion, cc-by-nc)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • HighWire Press Open Archive (submittedVersion)
Funders
National Health and Medical Research
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
Keywords
consensus design, protein stability, homologous protein sequences, evolutionary information, amino acid conservation, protein engineering
MeSH terms
Amino Acid Sequence, Animals, Humans, Proteins, Temperature, Thermodynamics, Protein Engineering, Sequence Alignment, Informatics, Protein Stability

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