The fact that cleavage of single peptide linkages in proteins often leads to extensive
conformational alteration, including regions far removed from the cleavage site is not fully …

Despite much progress in molecular biology, biophysics, and biochemistry, the mechanisms
by which unfolded polypeptide chains gain their native conformation are not yet fully …

We have examined the influence of surface hydrogen bonds on the stability of proteins by
studying the effects of mutations of human immunoglobulin light chain variable domain (VL) …

The significant contribution of disulfide bonds to the conformational stability of proteins is
generally considered to result from an entropic destabilization of the unfolded state causing …

Several recent studies have shown that it is possible to increase protein stability by
improving electrostatic interactions among charged groups on the surface of the folded …

Engineering proteins to withstand a broad range of conditions continues to be a coveted
objective, holding the potential to advance biomedicine, industry, and our understanding of …

The global and local stabilities of a eukaryotic ferricytochrome c variant with an engineered
disulfide are examined. The disulfide connects position 20, which is usually a valine, to …

A goal of protein engineering technology is developing methods to increase protein stability.
However, rational design of stable proteins is difficult because the stabilization mechanism …

The presented analysis concerns the inter-domain and inter-protein interface in protein
complexes. We propose extending the traditional understanding of the protein domain as a …

A simple theoretical model for increasing the protein stability by adequately redesigning the
distribution of charged residues on the surface of the native protein was tested …