ArticleProceedings of the National Academy of Sciences of the United States of America2008
Bioinformatic method for protein thermal stabilization by structural entropy optimization.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed.
- Rational Design of Adenylate Kinase Thermostability through Coevolution and Sequence Divergence Analysis.International journal of molecular sciences · 2021Article
- Parallel molecular mechanisms for enzyme temperature adaptation.Science (New York, N.Y.) · 2021Article
- Structural and mutational analyses of psychrophilic and mesophilic adenylate kinases highlight the role of hydrophobic interactions in protein thermal stability.Structural dynamics (Melville, N.Y.) · 2019Article
- Structural analyses of adenylate kinases from Antarctic and tropical fishes for understanding cold adaptation of enzymes.Scientific reports · 2017Article
- Improving the Thermostability and Activity of a Thermophilic Subtilase by Incorporating Structural Elements of Its Psychrophilic Counterpart.Applied and environmental microbiology · 2015Article
- Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Chemical Society reviews · 2015Review
- Stability curve prediction of homologous proteins using temperature-dependent statistical potentials.PLoS computational biology · 2014Article
- Protein thermostability prediction within homologous families using temperature-dependent statistical potentials.PloS one · 2014Article
- Detection and characterisation of mutations responsible for allele-specific protein thermostabilities at the Mn-superoxide dismutase gene in the deep-sea hydrothermal vent polychaete Alvinella pompejana.Journal of molecular evolution · 2013Article
- Article
- PROTS: a fragment based protein thermo-stability potential.Proteins · 2012Article
- Interconversion of functional motions between mesophilic and thermophilic adenylate kinases.PLoS computational biology · 2011Article
- Experimental evolution of adenylate kinase reveals contrasting strategies toward protein thermostability.Biophysical journal · 2010Article
- Predicting changes in protein thermostability brought about by single- or multi-site mutations.BMC bioinformatics · 2010Article
- Structure and biochemical characterization of an adenylate kinase originating from the psychrophilic organism Marinibacillus marinus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Describing protein conformational ensembles: beyond static snapshots.F1000 biology reports · 2009Article
- Optimal design of thermally stable proteins.Bioinformatics (Oxford, England) · 2008Article
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3 authors.
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Abstract
Engineering proteins for higher thermal stability is an important and difficult challenge. We describe a bioinformatic method incorporating sequence alignments to redesign proteins to be more stable through optimization of local structural entropy. Using this method, improved configurational entropy (ICE), we were able to design more stable variants of a mesophilic adenylate kinase with only the sequence information of one psychrophilic homologue. The redesigned proteins display considerable increases in their thermal stabilities while still retaining catalytic activity. ICE does not require a three-dimensional structure or a large number of homologous sequences, indicating a broad applicability of this method. Our results also highlight the importance of entropy in the stability of protein structures.
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