Separability between overall and internal motion: a protein folding problem
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Updated: May 19, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
1Department of Chemistry and Physical Sciences, College of Mount St. Joseph, Cincinnati, OH 45233, USA. eric_johnson@mail.msj.edu
Abstract:
The separability between overall and internal motions is evaluated over multiple folding trajectories of the villin headpiece subdomain. The analysis, which relies on the Prompers-Brüschweiler separability index, offers a potentially useful perspective on protein folding. The protein is considered folded in this study, not when it reaches some static target, but rather when it tumbles as a dynamically constrained object. The analysis also demonstrates how the separability index, when applied to protein folding simulations, can facilitate the analysis of NMR relaxation data.
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