Low growth temperatures improve the conformational quality of aggregation prone recombinant proteins in both soluble and insoluble <it>E. coli </it>cell fractions

Low growth temperatures improve the conformational quality of aggregation prone recombinant proteins in both soluble and insoluble <it>E. coli </it>cell fractions

Bibliographic Details
Main Authors: Villaverde Antonio, Arís Anna, Garcia-Fruitós Elena, González-Montalbán Núria, Vera Andrea
Format: Article
Language:English
Published: BMC 2006-10-01
Series:Microbial Cell Factories
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spelling doaj-7079078806a449da92bba1cb944713442020-11-25T01:10:20ZengBMCMicrobial 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
collection DOAJ
language English
format Article
sources DOAJ
author Villaverde Antonio
Arís Anna
Garcia-Fruitós Elena
González-Montalbán Núria
Vera 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
author_facet Villaverde Antonio
Arís Anna
Garcia-Fruitós Elena
González-Montalbán Núria
Vera Andrea
author_sort Villaverde Antonio
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_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_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_sort low growth temperatures improve the conformational quality of aggregation prone recombinant proteins in both soluble and insoluble <it>e. coli </it>cell fractions
publisher BMC
series Microbial Cell Factories
issn 1475-2859
publishDate 2006-10-01
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AT arisanna lowgrowthtemperaturesimprovetheconformationalqualityofaggregationpronerecombinantproteinsinbothsolubleandinsolubleitecoliitcellfractions
AT garciafruitoselena lowgrowthtemperaturesimprovetheconformationalqualityofaggregationpronerecombinantproteinsinbothsolubleandinsolubleitecoliitcellfractions
AT gonzalezmontalbannuria lowgrowthtemperaturesimprovetheconformationalqualityofaggregationpronerecombinantproteinsinbothsolubleandinsolubleitecoliitcellfractions
AT veraandrea lowgrowthtemperaturesimprovetheconformationalqualityofaggregationpronerecombinantproteinsinbothsolubleandinsolubleitecoliitcellfractions
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