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Sugar-induced molten-globule model

P R Davis-Searles¹, A S Morar, A J Saunders

¹Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-3290, USA.

|December 4, 1998

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Neutral sugars can stabilize acid-denatured proteins, inducing a collapsed A-state conformation similar to the molten globule. This effect, observed in equine ferricytochrome c, is attributed to steric repulsion between protein and sugar molecules.

Area of Science:

Biochemistry
Structural Biology
Protein Folding

Background:

Proteins denature at low pH due to intramolecular electrostatic repulsions.
Salt addition can induce a collapsed A-state, resembling a molten globule intermediate.

Purpose of the Study:

To investigate the effect of neutral sugars on acid-denatured equine ferricytochrome c.
To determine if sugars can induce the A-state in the absence of salt.

Main Methods:

Circular dichroism spectropolarimetry (CD) for structural characterization.
NMR-monitored hydrogen-deuterium exchange for stability assessment.
Analysis of sugar size and concentration effects on protein stability.

Main Results:

Related Experiment Videos

Neutral sugars induced the A-state in acid-denatured equine ferricytochrome c without added salt.
The stability of the sugar-induced A-state was dependent on sugar size and concentration.
Structural and stability data were consistent with increased steric repulsion.

Conclusions:

Neutral sugars can stabilize partially folded protein states.
Steric repulsion between protein and sugar molecules is the likely mechanism for stabilization.
This finding offers insights into protein folding intermediates and stabilization strategies.