Thermostable exoshells fold and stabilize recombinant proteins

10.1038/s41467-017-01585-2

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Main Authors:	Deshpande S., Masurkar N.D., Girish V.M., Desai M., Chakraborty G., Chan J.M., Drum C.L.
Other Authors:	MEDICINE
Format:	Article
Published:	Nature Publishing Group 2020
Subjects:	green fluorescent protein horseradish peroxidase nanoparticle recombinant protein Renilla luciferin 2 monooxygenase thermostable protein nanoparticle unclassified drug gene expression protein shell stabilization Article controlled study drug release drug stability enzyme substrate fluorescence in vitro study nanoencapsulation nanoengineering nanotechnology nonhuman pH protein degradation protein denaturation protein expression protein folding protein metabolism protein tertiary structure stereospecificity thermostability titrimetry Archaeoglobus fulgidus biosynthesis chemistry Escherichia coli genetics metabolism physiology Armoracia rusticana Renilla luciferase Gene Expression Green Fluorescent Proteins Horseradish Peroxidase Luciferases, Renilla Nanoparticles Protein Folding Recombinant Proteins
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/174485
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1744852024-11-15T08:51:42Z Thermostable exoshells fold and stabilize recombinant proteins Deshpande S. Masurkar N.D. Girish V.M. Desai M. Chakraborty G. Chan J.M. Drum C.L. MEDICINE SURGERY green fluorescent protein horseradish peroxidase nanoparticle recombinant protein Renilla luciferin 2 monooxygenase thermostable protein nanoparticle unclassified drug recombinant protein gene expression nanoparticle protein shell stabilization Article controlled study drug release drug stability enzyme substrate fluorescence in vitro study nanoencapsulation nanoengineering nanotechnology nonhuman pH protein degradation protein denaturation protein expression protein folding protein metabolism protein tertiary structure stereospecificity thermostability titrimetry Archaeoglobus fulgidus biosynthesis chemistry Escherichia coli gene expression genetics metabolism physiology protein folding Armoracia rusticana Renilla luciferase Archaeoglobus fulgidus Escherichia coli Gene Expression Green Fluorescent Proteins Horseradish Peroxidase Luciferases, Renilla Nanoparticles Protein Folding Recombinant Proteins 10.1038/s41467-017-01585-2 Nature Communications 8 1 1442 2020-09-06T16:03:55Z 2020-09-06T16:03:55Z 2017 Article Deshpande 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 2041-1723 https://scholarbank.nus.edu.sg/handle/10635/174485 Nature Publishing Group Unpaywall 20200831
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	green fluorescent protein horseradish peroxidase nanoparticle recombinant protein Renilla luciferin 2 monooxygenase thermostable protein nanoparticle unclassified drug recombinant protein gene expression nanoparticle protein shell stabilization Article controlled study drug release drug stability enzyme substrate fluorescence in vitro study nanoencapsulation nanoengineering nanotechnology nonhuman pH protein degradation protein denaturation protein expression protein folding protein metabolism protein tertiary structure stereospecificity thermostability titrimetry Archaeoglobus fulgidus biosynthesis chemistry Escherichia coli gene expression genetics metabolism physiology protein folding Armoracia rusticana Renilla luciferase Archaeoglobus fulgidus Escherichia coli Gene Expression Green Fluorescent Proteins Horseradish Peroxidase Luciferases, Renilla Nanoparticles Protein Folding Recombinant Proteins
spellingShingle	green fluorescent protein horseradish peroxidase nanoparticle recombinant protein Renilla luciferin 2 monooxygenase thermostable protein nanoparticle unclassified drug recombinant protein gene expression nanoparticle protein shell stabilization Article controlled study drug release drug stability enzyme substrate fluorescence in vitro study nanoencapsulation nanoengineering nanotechnology nonhuman pH protein degradation protein denaturation protein expression protein folding protein metabolism protein tertiary structure stereospecificity thermostability titrimetry Archaeoglobus fulgidus biosynthesis chemistry Escherichia coli gene expression genetics metabolism physiology protein folding Armoracia rusticana Renilla luciferase Archaeoglobus fulgidus Escherichia coli Gene Expression Green Fluorescent Proteins Horseradish Peroxidase Luciferases, Renilla Nanoparticles Protein Folding Recombinant Proteins Deshpande S. Masurkar N.D. Girish V.M. Desai M. Chakraborty G. Chan J.M. Drum C.L. Thermostable exoshells fold and stabilize recombinant proteins
description	10.1038/s41467-017-01585-2
author2	MEDICINE
author_facet	MEDICINE Deshpande S. Masurkar N.D. Girish V.M. Desai M. Chakraborty G. Chan J.M. Drum C.L.
format	Article
author	Deshpande S. Masurkar N.D. Girish V.M. Desai M. Chakraborty G. Chan J.M. Drum C.L.
author_sort	Deshpande S.
title	Thermostable exoshells fold and stabilize recombinant proteins
title_short	Thermostable exoshells fold and stabilize recombinant proteins
title_full	Thermostable exoshells fold and stabilize recombinant proteins
title_fullStr	Thermostable exoshells fold and stabilize recombinant proteins
title_full_unstemmed	Thermostable exoshells fold and stabilize recombinant proteins
title_sort	thermostable exoshells fold and stabilize recombinant proteins
publisher	Nature Publishing Group
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/174485
_version_	1821181354878959616

Thermostable exoshells fold and stabilize recombinant proteins

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