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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

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Published on: April 28, 2011

How important is the molten globule for correct protein folding?

T E Creighton¹

¹European Molecular Biology Laboratory, Heidelberg, Germany. creighton@embl-heidelberg.de

Trends in Biochemical Sciences

|January 1, 1997

Summary

The molten globule state may not be a native-like protein folding intermediate. Experimental data suggest its topology is not crucial for rapid protein folding.

Area of Science:

Biochemistry
Protein Folding Dynamics
Structural Biology

Background:

The molten globule (MG) state is traditionally viewed as a key intermediate in protein folding.
This perspective is largely based on studies of MG proteins with native-like constraints.

Purpose of the Study:

To re-evaluate the native-like topology of the molten globule state.
To determine the role of the MG state in rapid protein folding.

Main Methods:

Investigated alpha-lactalbumin's molten globule state.
Allowed disulfide bonds to rearrange to favor MG topology.
Analyzed experimental data on protein folding intermediates.

Main Results:

Opposite conclusions were obtained when disulfide bonds rearranged.

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The MG state's native-like topology was found to be negligible.

The MG state is not essential for rapid protein folding.

Conclusions:

The molten globule state's topology is not significantly native-like.
The molten globule state does not appear to be the key to rapid protein folding.