title: Stability and co-operative properties of partially folded proteins.
abstract: Biophysical and thermodynamic properties of various partially folded forms of proteins are considered which can be obtained by (a) removal of prosthetic groups, (b) acid denaturation, (c) melting of subdomain-containing proteins, and (d) selective cleavage of disulfides. The examples of alpha-lactalbumin and myoglobin will be discussed in more detail. The existence of both co-operative and gradual transitions is shown. The results do not support the idea that the molten globule represents a distinct thermodynamic state.
authors.affiliation: Institute of Biochemistry and Molecular Physiology, University of Potsdam, c/o Max-Delbrück-Center, Robert-Rössle-Str. 10, D-13125 Berlin-Buch, Germany. wpfeil@orion.rz.mdc-berlin.de
authors.forename: W
authors.initials: W
authors.lastname: Pfeil
mesh_terms: D000818:Animals; D004355:Drug Stability; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D013816:Thermodynamics