Refolding of Proteins From Inclusion Bodies Is Favored by a Diminished Hydrophobic Effect at Elevated Pressures
Journal Article
Overview
publication date
- February 1, 2009
has subject area
- Bacteriophages - Bacteriophage T4
- Biochemical Phenomena - Protein Biosynthesis
- Biochemical Phenomena - Protein Folding
- Biological Science Disciplines - Biotechnology
- Biophysical Phenomena - Protein Folding
- DNA Viruses - Bacteriophage T4
- Gammaproteobacteria - Escherichia coli
- Gene Expression - Protein Biosynthesis
- Gram-Negative Facultatively Anaerobic Rods - Escherichia coli
- Guanidine
- Hydrophobic and Hydrophilic Interactions
- Hydrostatic Pressure
- Inclusion Bodies
- Investigative Techniques - Enzyme Stability
- Metabolism - Protein Biosynthesis
- Muramidase
- Protein Conformation
- Protein Stability - Enzyme Stability
- Recombinant Proteins
- T-Phages - Bacteriophage T4
- Technology - Biotechnology
- Thermodynamics
has restriction
- closed
Date in CU Experts
- September 3, 2013 2:48 AM
Full Author List
- Crisman RI; Randolph TW
author count
- 2
citation count
- 35
published in
- Biotechnology and Bioengineering Journal
Other Profiles
International Standard Serial Number (ISSN)
- 0006-3592
Electronic International Standard Serial Number (EISSN)
- 1097-0290
Digital Object Identifier (DOI)
Additional Document Info
start page
- 483
end page
- 492
volume
- 102
issue
- 2