Proteins are now widely produced in diverse microbial cell factories. The Escherichia coli is
still the dominant host for recombinant protein production but, as a bacterial cell, it also has …

The mechanism of protein folding (represented schematically below) is one of the most
fascinating problems in the field of chemical reactions. This review presents the progess …

Many small, monomeric proteins fold with simple two-state kinetics and show wide variation
in folding rates, from microseconds to seconds. Thus, stable intermediates are not a …

SUMO (small ubiquitin-related modifier) modulates protein structure and function by
covalently binding to the lysine side chains of the target proteins. Yeast cells contain two …

The demands of structural and functional genomics for large quantities of soluble, properly
folded proteins in heterologous hosts have been aided by advancements in the field of …

Despite the availability of numerous gene fusion systems, recombinant protein expression in
Escherichia coli remains difficult. Establishing the best fusion partner for difficult‐to‐express …

An elementary statistical mechanical model was used to calculate the folding rates for 22
proteins from their known three-dimensional structures. In this model, residues come into …

The ability of protein molecules to fold into their highly structured functional states is one of
the most remarkable evolutionary achievements of biology. In recent years, our …

We used force-clamp atomic force micoscopy to measure the end-to-end length of the small
protein ubiquitin during its folding reaction at the single-molecule level. Ubiquitin was first …

Equilibrium molecular dynamics simulations, in which proteins spontaneously and
repeatedly fold and unfold, have recently been used to help elucidate the mechanistic …