Evidence map›Paper›PMID 29087185›Full record

ArticleBiochemistry2017

Comparison of Five Protein Engineering Strategies for Stabilizing an α/β-Hydrolase.

Bryan J Jones, Huey Yee Lim, Jun Huang, Romas J Kazlauskas

Abstract readComparative Study
In one paragraph

Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Engineering Protein Dynamics through Mutational Energy Landscape Traps.Journal of chemical information and modeling · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Protein Stability: Enhancement and Measurement.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  10. Article
  11. Leveraging intrinsic flexibility to engineer enhanced enzyme catalytic activity.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Engineering and evaluation of thermostableEngineering in life sciences · 2022
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Consensus Design of an Evolved High-Redox Potential Laccase.Frontiers in bioengineering and biotechnology · 2020
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Bryan J JonesDepartment of Biochemistry, Molecular Biology & Biophysics and The Biotechnology Institute, University of Minnesota , 1479 Gortner Avenue, Saint Paul, Minnesota 55108, United States.
Huey Yee LimDepartment of Biochemistry, Molecular Biology & Biophysics and The Biotechnology Institute, University of Minnesota , 1479 Gortner Avenue, Saint Paul, Minnesota 55108, United States.
Jun HuangDepartment of Biochemistry, Molecular Biology & Biophysics and The Biotechnology Institute, University of Minnesota , 1479 Gortner Avenue, Saint Paul, Minnesota 55108, United States.
Romas J KazlauskasDepartment of Biochemistry, Molecular Biology & Biophysics and The Biotechnology Institute, University of Minnesota , 1479 Gortner Avenue, Saint Paul, Minnesota 55108, United States.ORCID http://orcid.org/0000-0002-3570-2411

Funding

TRAINING FOR FUTURE BIOTECHNOLOGY DEVELOPMENTT32GM008347 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI SCHMIDT-DANNERT, CLAUDIA · 1990 to 2021
$11.0M
Evolutionary Insights Into Enzyme MechanismsR01GM102205 · NIGMS · UNIVERSITY OF MINNESOTA · PI DEAN, ANTONY M., KAZLAUSKAS, ROMAS J · 2012 to 2015
$1.8M
NIGMS NIH HHS R01 GM102205NIGMS NIH HHS T32 GM008347
6 · The paper itself

Abstract

A review of the previous stabilization of α/β-hydrolase fold enzymes revealed many different strategies, but no comparison of strategies on the same enzyme. For this reason, we compared five strategies to identify stabilizing mutations in a model α/β-hydrolase fold enzyme, salicylic acid binding protein 2, to reversible denaturation by urea and to irreversible denaturation by heat. The five strategies included one location agnostic approach (random mutagenesis using error-prone polymerase chain reaction), two structure-based approaches [computational design (Rosetta, FoldX) and mutation of flexible regions], and two sequence-based approaches (addition of proline at locations where a more stable homologue has proline and mutation to consensus). All strategies identified stabilizing mutations, but the best balance of success rate, degree of stabilization, and ease of implementation was mutation to consensus. A web-based automated program that predicts substitutions needed to mutate to consensus is available at http://kazlab.umn.edu .

Indexed as

Amino Acid SequenceBase SequenceCrystallography, X-RayEnzyme StabilityHydrolasesModels, MolecularMutagenesisMutationPoint MutationProtein EngineeringProteinsHydrolasesProteins

Identifiers

PMID29087185
PMCPMC5736438

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.