Stability and co-operative properties of partially folded proteins.
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.
Pfeil
W
W
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
D000818:Animals; D004355:Drug Stability; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D013816:Thermodynamics