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 …

The folding of many newly synthesized proteins in the cell depends on a set of conserved
proteins known as molecular chaperones. These prevent the formation of misfolded protein …

Existing variants of green fluorescent protein (GFP) often misfold when expressed as fusions
with other proteins. We have generated a robustly folded version of GFP …

The His274→ Tyr274 (H274Y) mutation confers oseltamivir resistance on N1 influenza
neuraminidase but had long been thought to compromise viral fitness. However, beginning …

Aggregation results in the formation of inclusion bodies, amyloid fibrils and folding
aggregates. Substantial data support the hypothesis that partially folded intermediates are …

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 …

The folding of most newly synthesized proteins in the cell requires the interaction of a variety
of protein cofactors known as molecular chaperones. These molecules recognize and bind …

Proteins are finicky molecules; they are barely stable and are prone to aggregate, but they
must function in a crowded environment that is full of degradative enzymes bent on their …

Proteins, due to the delicate balance of stabilizing and destabilizing interactions, are only
marginally stable. Adaptation to extreme environments tends to shift the 'mesophilic' …

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 …