The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures
Author:
Publisher
Wiley
Subject
Applied Microbiology and Biotechnology,Bioengineering,Biotechnology
Reference35 articles.
1. FT-IR study of heterologous protein expression in recombinant Escherichia coli strains
2. Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy
3. Structural analysis of protein inclusion bodies by Fourier transform infrared microspectroscopy
4. Temperature dependence of the hydrophobic interaction in protein folding.
5. Recombinant protein folding and misfolding in Escherichia coli
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