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 …

Proteins carry out the most important and difficult tasks in all living organisms. To do so, they
must often interact specifically with other small and large molecules. This requires that they …

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 …

抄録< jats: title> Abstract</jats: title>< jats: p> The stability of proteins, especially enzymes,
has long been a practical concern (1), because this is usually the factor that most limits their …

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 …