Preparations enriched by a specific protein are rarely easily obtained from natural host cells.
Hence, recombinant protein production is frequently the sole applicable procedure. The …

Pure, soluble and functional proteins are of high demand in modern biotechnology. Natural
protein sources rarely meet the requirements for quantity, ease of isolation or price and …

The vast expansion of protein sequence databases provides an opportunity for new protein
design approaches which seek to learn the sequence-function relationship directly from …

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 …

Motivation Protein solubility plays a vital role in pharmaceutical research and production
yield. For a given protein, the extent of its solubility can represent the quality of its function …

The secretory production of recombinant proteins by the Gram-negative bacterium
Escherichia coli has several advantages over intracellular production as inclusion bodies. In …

Increasing a protein concentration in solution to the required level, without causing
aggregation and precipitation is often a challenging but important task, especially in the field …

An algorithm for the automated macromolecular model building of polypeptide backbones is
described. The procedure is hierarchical. In the initial stages, many overlapping polypeptide …

The efficiency and high specificity of tobacco etch virus (TEV) protease has made it widely
used for cleavage of recombinant fusion proteins. However, the production of TEV protease …

Functional and structural studies of membrane proteins usually require overexpression of
the proteins in question. Often, however, the 'trial and error'approaches that are mainly used …