The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum.
We have observed that a soluble recombinant green fluorescent protein produced in Escherichia coli occurs in a wide conformational spectrum. This results in differently fluorescent protein fractions in which morphologically diverse soluble aggregates abound. Therefore, the functional quality of solu...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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2008
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| _version_ | 1826280180634615808 |
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| author | Martínez-Alonso, M González-Montalbán, N García-Fruitós, E Villaverde, A |
| author_facet | Martínez-Alonso, M González-Montalbán, N García-Fruitós, E Villaverde, A |
| author_sort | Martínez-Alonso, M |
| collection | OXFORD |
| description | We have observed that a soluble recombinant green fluorescent protein produced in Escherichia coli occurs in a wide conformational spectrum. This results in differently fluorescent protein fractions in which morphologically diverse soluble aggregates abound. Therefore, the functional quality of soluble versions of aggregation-prone recombinant proteins is defined statistically rather than by the prevalence of a canonical native structure. |
| first_indexed | 2024-03-07T00:09:51Z |
| format | Journal article |
| id | oxford-uuid:78dc2a57-6bed-4f22-9411-f31848b46e52 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T00:09:51Z |
| publishDate | 2008 |
| record_format | dspace |
| spelling | oxford-uuid:78dc2a57-6bed-4f22-9411-f31848b46e522022-03-26T20:33:23ZThe Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:78dc2a57-6bed-4f22-9411-f31848b46e52EnglishSymplectic Elements at Oxford2008Martínez-Alonso, MGonzález-Montalbán, NGarcía-Fruitós, EVillaverde, AWe have observed that a soluble recombinant green fluorescent protein produced in Escherichia coli occurs in a wide conformational spectrum. This results in differently fluorescent protein fractions in which morphologically diverse soluble aggregates abound. Therefore, the functional quality of soluble versions of aggregation-prone recombinant proteins is defined statistically rather than by the prevalence of a canonical native structure. |
| spellingShingle | Martínez-Alonso, M González-Montalbán, N García-Fruitós, E Villaverde, A The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum. |
| title | The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum. |
| title_full | The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum. |
| title_fullStr | The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum. |
| title_full_unstemmed | The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum. |
| title_short | The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum. |
| title_sort | functional quality of soluble recombinant polypeptides produced in escherichia coli is defined by a wide conformational spectrum |
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