Complex processes are involved in the protection of cells and organisms by heat shock
proteins (hsps). Aberrant protein production due to high temperatures is prevented by the …

The experimental material accumulated in the literature on the conformational behavior of
intrinsically unstructured (natively unfolded) proteins was analyzed. Results of this analysis …

Albumin, the most abundant plasma protein, is among the most studied of all proteins, being
important from clinical monitoring, physiological, and therapeutic perspectives. This unique …

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 …

Noncovalent, extrinsic fluorescent dyes are applied in various fields of protein analysis, eg to
characterize folding intermediates, measure surface hydrophobicity, and detect aggregation …

The most commonly occurring intrinsically disordered proteins (IDPs) are polyampholytes,
which are defined by the duality of low net charge per residue and high fractions of charged …

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 …

Pulse field gradient NMR methods have been used to determine the effective hydrodynamic
radii of a range of native and nonnative protein conformations. From these experimental …

General principles of protein structure, stability, and folding kinetics have recently been
explored in computer simulations of simple exact lattice models. These models represent …

Carbonic anhydrase (CA, EC 4.2. 1.1) is a protein that is especially well-suited to serve as a
model in many types of studies in biophysics, bioanalysis, the physical-organic chemistry of …