Related Experiment Video
Updated: Aug 24, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
Critical nucleation size in the folding of small apparently two-state proteins
Yawen Bai1, Hongyi Zhou, Yaoqi Zhou
1Laboratory of Biochemistry, National Cancer Institute, NIH, Bethesda, Maryland 20892, USA. yawen@helix.nih.gov
Abstract:
For apparently two-state proteins, we found that the size (number of folded residues) of a transition state is mostly encoded by the topology, defined by total contact distance (TCD) of the native state, and correlates with its folding rate. This is demonstrated by using a simple procedure to reduce the native structures of the 41 two-state proteins with native TCD as a constraint, and is further supported by analyzing the results of eight proteins from protein engineering studies. These results support the hypothesis that the major rate-limiting process in the folding of small apparently two-state proteins is the search for a critical number of residues with the topology close to that of the native state.
Related Concept Videos
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Molecular Chaperones and Protein Folding
The...
Nuclear Protein Sorting
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
Pinching-off of Coated Vesicles
Bacterial Protein Maturation

