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Updated: Aug 21, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
The role of sequence and structure in protein folding kinetics; the diffusion-collision model applied to proteins L
Suhail A Islam1, Martin Karplus, David L Weaver
1Structural Bioinformatics Group, Department of Biological Sciences, Biochemistry Building, Imperial College of Science, Technology and Medicine, London SW7 2AY, United Kingdom.
Abstract:
The diffusion-collision model (DCM) is applied to the folding kinetics of protein L and protein G. In the DCM, the two proteins are treated as consisting of two beta-hairpins and one alpha-helix, so that they are isomorphous with the three-helix bundle DCM model. In the absence of sequence dependent factors, both proteins would fold in the same way in the DCM, with the coalescence of the N-terminal hairpin and the helix slightly favored over the C-terminal hairpin and the helix because the former are closer together than the latter. However, sequence dependent factors make the N-terminal hairpin of protein L and the C-terminal hairpin of protein G more stable in the ensemble of unfolded conformations. This difference in the stabilities gives rise to the difference in the calculated folding behavior, in agreement with experiment.
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