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Updated: Sep 27, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
Is there a unifying mechanism for protein folding?
Valerie Daggett1, Alan R Fersht
1Department of Medicinal Chemistry, University of Washington, Seattle, WA 98195-7610, USA. daggett@u.washington.edu
Abstract:
Proteins appear to fold by diverse pathways, but variations of a simple mechanism - nucleation-condensation - describe the overall features of folding of most domains. In general, secondary structure is inherently unstable and its stability is enhanced by tertiary interactions. Consequently, an extensive interplay of secondary and tertiary interactions determines the transition-state for folding, which is structurally similar to the native state, being formed in a general collapse (condensation) around a diffuse nucleus. As the propensity for stable secondary structure increases, folding becomes more hierarchical and eventually follows a framework mechanism where the transition state is assembled from pre-formed secondary structural elements.
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