REVIEW: Stability and Co-operative Properties of Partially Folded Proteins

W. Pfeil

Institute of Biochemistry and Molecular Physiology, University of Potsdam, c/o Max-Delbrück-Center, Robert-Rössle-Str. 10, D-13125 Berlin-Buch, Germany; fax: +49-30-9489-3744; E-mail: wpfeil@orion.rz.mdc-berlin.de

Received June 23, 1997

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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.

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KEY WORDS: alpha-lactalbumin, myoglobin, thermodynamics of protein denaturation, differential scanning calorimetry, circular dichroism

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