[HTML][HTML] Theory and applications of differential scanning fluorimetry in early-stage drug discovery
K Gao, R Oerlemans, MR Groves - Biophysical reviews, 2020 - Springer
Differential scanning fluorimetry (DSF) is an accessible, rapid, and economical biophysical
technique that has seen many applications over the years, ranging from protein folding state …
technique that has seen many applications over the years, ranging from protein folding state …
[HTML][HTML] Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process
Formation of inclusion bodies in bacterial hosts poses a major challenge for large scale
recovery of bioactive proteins. The process of obtaining bioactive protein from inclusion …
recovery of bioactive proteins. The process of obtaining bioactive protein from inclusion …
[HTML][HTML] Recombinant protein expression in Escherichia coli: advances and challenges
GL Rosano, EA Ceccarelli - Frontiers in microbiology, 2014 - frontiersin.org
Escherichia coli is one of the organisms of choice for the production of recombinant proteins.
Its use as a cell factory is well-established and it has become the most popular expression …
Its use as a cell factory is well-established and it has become the most popular expression …
Strategies for improving antimicrobial peptide production
Antimicrobial peptides (AMPs) found in a wide range of animal, insect, and plant species are
host defense peptides forming an integral part of their innate immunity. Although the exact …
host defense peptides forming an integral part of their innate immunity. Although the exact …
Solubilization and refolding of bacterial inclusion body proteins
SM Singh, AK Panda - Journal of bioscience and bioengineering, 2005 - Elsevier
Inclusion bodies produced in Escherichia coli are composed of densely packed denatured
protein molecules in the form of particles. Refolding of inclusion body proteins into bioactive …
protein molecules in the form of particles. Refolding of inclusion body proteins into bioactive …
Rationalization of the effects of mutations on peptide andprotein aggregation rates
In order for any biological system to function effectively, it is essential to avoid the inherent
tendency of proteins to aggregate and form potentially harmful deposits,,,. In each of the …
tendency of proteins to aggregate and form potentially harmful deposits,,,. In each of the …
Recombinant protein secretion in Escherichia coli
FJM Mergulhão, DK Summers, GA Monteiro - Biotechnology advances, 2005 - Elsevier
The secretory production of recombinant proteins by the Gram-negative bacterium
Escherichia coli has several advantages over intracellular production as inclusion bodies. In …
Escherichia coli has several advantages over intracellular production as inclusion bodies. In …
Recombinant protein expression: challenges in production and folding related matters
Protein folding is a biophysical process by which proteins reach a specific three-dimensional
structure. The amino acid sequence of a polypeptide chain contains all the information …
structure. The amino acid sequence of a polypeptide chain contains all the information …
Lysozyme: a model protein for amyloid research
Ever since lysozyme was discovered by Fleming in 1922, this protein has emerged as a
model for investigations on protein structure and function. Over the years, several high …
model for investigations on protein structure and function. Over the years, several high …
Protein aggregation in recombinant bacteria: biological role of inclusion bodies
A Villaverde, M Mar Carrió - Biotechnology letters, 2003 - Springer
Protein aggregation is an ordinary consequence of thermal stress. In recombinant bacteria,
the over-expression of plasmid-encoded genes triggers transcription of heat-shock genes …
the over-expression of plasmid-encoded genes triggers transcription of heat-shock genes …