Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41467-017-01585-2
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dc.titleThermostable exoshells fold and stabilize recombinant proteins
dc.contributor.authorDeshpande S.
dc.contributor.authorMasurkar N.D.
dc.contributor.authorGirish V.M.
dc.contributor.authorDesai M.
dc.contributor.authorChakraborty G.
dc.contributor.authorChan J.M.
dc.contributor.authorDrum C.L.
dc.date.accessioned2020-09-06T16:03:55Z
dc.date.available2020-09-06T16:03:55Z
dc.date.issued2017
dc.identifier.citationDeshpande S., Masurkar N.D., Girish V.M., Desai M., Chakraborty G., Chan J.M., Drum C.L. (2017). Thermostable exoshells fold and stabilize recombinant proteins. Nature Communications 8 (1) : 1442. ScholarBank@NUS Repository. https://doi.org/10.1038/s41467-017-01585-2
dc.identifier.issn2041-1723
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/174485
dc.description.abstractThe expression and stabilization of recombinant proteins is fundamental to basic and applied biology. Here we have engineered a thermostable protein nanoparticle (tES) to improve both expression and stabilization of recombinant proteins using this technology. tES provides steric accommodation and charge complementation to green fluorescent protein (GFPuv), horseradish peroxidase (HRPc), and Renilla luciferase (rLuc), improving the yields of functional in vitro folding by ~100-fold. Encapsulated enzymes retain the ability to metabolize small-molecule substrates, presumably via four 4.5-nm pores present in the tES shell. GFPuv exhibits no spectral shifts in fluorescence compared to a nonencapsulated control. Thermolabile proteins internalized by tES are resistant to thermal, organic, chaotropic, and proteolytic denaturation and can be released from the tES assembly with mild pH titration followed by proteolysis. © 2017 The Author(s).
dc.publisherNature Publishing Group
dc.sourceUnpaywall 20200831
dc.subjectgreen fluorescent protein
dc.subjecthorseradish peroxidase
dc.subjectnanoparticle
dc.subjectrecombinant protein
dc.subjectRenilla luciferin 2 monooxygenase
dc.subjectthermostable protein nanoparticle
dc.subjectunclassified drug
dc.subjectrecombinant protein
dc.subjectgene expression
dc.subjectnanoparticle
dc.subjectprotein
dc.subjectshell
dc.subjectstabilization
dc.subjectArticle
dc.subjectcontrolled study
dc.subjectdrug release
dc.subjectdrug stability
dc.subjectenzyme substrate
dc.subjectfluorescence
dc.subjectin vitro study
dc.subjectnanoencapsulation
dc.subjectnanoengineering
dc.subjectnanotechnology
dc.subjectnonhuman
dc.subjectpH
dc.subjectprotein degradation
dc.subjectprotein denaturation
dc.subjectprotein expression
dc.subjectprotein folding
dc.subjectprotein metabolism
dc.subjectprotein tertiary structure
dc.subjectstereospecificity
dc.subjectthermostability
dc.subjecttitrimetry
dc.subjectArchaeoglobus fulgidus
dc.subjectbiosynthesis
dc.subjectchemistry
dc.subjectEscherichia coli
dc.subjectgene expression
dc.subjectgenetics
dc.subjectmetabolism
dc.subjectphysiology
dc.subjectprotein folding
dc.subjectArmoracia rusticana
dc.subjectRenilla luciferase
dc.subjectArchaeoglobus fulgidus
dc.subjectEscherichia coli
dc.subjectGene Expression
dc.subjectGreen Fluorescent Proteins
dc.subjectHorseradish Peroxidase
dc.subjectLuciferases, Renilla
dc.subjectNanoparticles
dc.subjectProtein Folding
dc.subjectRecombinant Proteins
dc.typeArticle
dc.contributor.departmentDEPT OF MEDICINE
dc.contributor.departmentDEPT OF SURGERY
dc.description.doi10.1038/s41467-017-01585-2
dc.description.sourcetitleNature Communications
dc.description.volume8
dc.description.issue1
dc.description.page1442
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