The natural habitat of most proteins is an aqueous environment. Nevertheless, when a
protein solution is contacted with another phase (either a solid, liquid, or gas) with which it is …

Ageritin is a specific ribonuclease, extracted from the edible mushroom Cyclocybe aegerita
(synonym Agrocybe aegerita), which cleaves a single phosphodiester bond located within …

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 …

We thank Dr. RA Stockley of The General Hospital of The University of Birmingham, United
Kingdom, for providing us with sheep anti-human aj-antichymotrypsin antibody, the nursing …

You must first decide which technique to use to follow unfolding. The techniques used most
often are UV difference spectroscopy, fluorescence and circular dichroism (CD), which are …

The question of how the primary amino acid sequence of a protein determines its three-
dimensional structure is still unanswered. One approach to this problem involves the de …

The objective of this study was to address the question of whether or not urea and guanidine
hydrochloride (GdnHCl) give the same estimates of the stability of a particular protein. We …

Ribonuclease T1 has two disulfide bonds linking cysteine residues 2-10 and 6-103. We
have prepared a derivative of ribonuclease T1 in which one disulfide bond is broken and the …

The functional properties of food proteins affect behavior in food systems and influence the
quality attributes, structure, texture, mouth-feel, and flavor of the final product. These …

Abstract Changes in excluded volume and contact interaction with the surface of a protein
have been suggested as mechanisms for the changes in stability induced by cosolvents …