The use of enzymes in industrial processes requires the improvement of their features in
many instances. Enzyme immobilization, a requirement to facilitate the recovery and reuse …

Water is an essential participant in the stability, structure, dynamics, and function of proteins
and other biomolecules. Thermodynamically, changes in the aqueous environment affect …

Denaturant m values, the dependence of the free energy of unfolding on denaturant
concentration, have been collected for a large set of proteins. The m value correlates very …

To elucidate the kinetic importance of structural intermediates in single-domain proteins, we
measured the effect of solution conditions and amino-acid changes at a central core residue …

Camelids produce functional “heavy chain” antibodies which are devoid of light chains and
CH1 domains [Hamers-Casterman, C., et al.(1993) Nature 363, 446− 448]. It has been …

Protein Folding Kinetics-Biophysical Methods (2nd Edition) gives a deep insight into the
principles and concepts of the kinetic and structural resolution of fast chemical and …

The urea, guanidine hydrochloride, salt, and temperature dependence of the rate of
dissociation of CO from a nonequilibrium state of CO-bound native ferrocytochrome c has …

The signal peptide plays a key role in targeting and membrane insertion of secretory and
membrane proteins in both prokaryotes and eukaryotes. In E. coli, recombinant proteins can …

Standard methods for measuring free energy of protein unfolding by chemical denaturation
require complete folding at low concentrations of denaturant so that a native baseline can be …

A monomolecular native‐like three‐helix bundle has been designed in an iterative process,
beginning with a peptide that noncooperatively assembled into an antiparallel three‐helix …