Low growth temperatures improve the conformational quality of aggregation prone recombinant proteins in both soluble and insoluble <it>E. coli </it>cell fractions
Main Authors: | , , , , |
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Format: | Article |
Language: | English |
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BMC
2006-10-01
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Series: | Microbial Cell Factories |
_version_ | 1818481630749130752 |
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author | Villaverde Antonio Arís Anna Garcia-Fruitós Elena González-Montalbán Núria Vera Andrea |
author_facet | Villaverde Antonio Arís Anna Garcia-Fruitós Elena González-Montalbán Núria Vera Andrea |
author_sort | Villaverde Antonio |
collection | DOAJ |
first_indexed | 2024-12-10T11:37:30Z |
format | Article |
id | doaj.art-7079078806a449da92bba1cb94471344 |
institution | Directory Open Access Journal |
issn | 1475-2859 |
language | English |
last_indexed | 2024-12-10T11:37:30Z |
publishDate | 2006-10-01 |
publisher | BMC |
record_format | Article |
series | Microbial Cell Factories |
spelling | doaj.art-7079078806a449da92bba1cb944713442022-12-22T01:50:23ZengBMCMicrobial Cell Factories1475-28592006-10-015Suppl 1P710.1186/1475-2859-5-S1-P7Low growth temperatures improve the conformational quality of aggregation prone recombinant proteins in both soluble and insoluble <it>E. coli </it>cell fractionsVillaverde AntonioArís AnnaGarcia-Fruitós ElenaGonzález-Montalbán NúriaVera Andrea |
spellingShingle | Villaverde Antonio Arís Anna Garcia-Fruitós Elena González-Montalbán Núria Vera Andrea Low growth temperatures improve the conformational quality of aggregation prone recombinant proteins in both soluble and insoluble <it>E. coli </it>cell fractions Microbial Cell Factories |
title | Low growth temperatures improve the conformational quality of aggregation prone recombinant proteins in both soluble and insoluble <it>E. coli </it>cell fractions |
title_full | Low growth temperatures improve the conformational quality of aggregation prone recombinant proteins in both soluble and insoluble <it>E. coli </it>cell fractions |
title_fullStr | Low growth temperatures improve the conformational quality of aggregation prone recombinant proteins in both soluble and insoluble <it>E. coli </it>cell fractions |
title_full_unstemmed | Low growth temperatures improve the conformational quality of aggregation prone recombinant proteins in both soluble and insoluble <it>E. coli </it>cell fractions |
title_short | Low growth temperatures improve the conformational quality of aggregation prone recombinant proteins in both soluble and insoluble <it>E. coli </it>cell fractions |
title_sort | low growth temperatures improve the conformational quality of aggregation prone recombinant proteins in both soluble and insoluble it e coli it cell fractions |
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