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Stability and co-operative properties of partially folded proteins
1Institute 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
Biochemistry. Biokhimiia
|June 4, 1998
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.