Predictions of protein flexibility: first-order measures
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Updated: Aug 23, 2026

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
Published on: April 25, 2025
Julio A Kovacs1, Pablo Chacón, Ruben Abagyan
1Department of Molecular Biology, The Scripps Research Institute La Jolla, California 92037, USA. jkovacs@scripps.edu
Abstract:
The normal modes of a molecule are utilized, in conjunction with classical conformal vector field theory, to define a function that measures the capability of the molecule to deform at each of its residues. An efficient algorithm is presented to calculate the local chain deformability from the set of normal modes of vibration. This is done by considering each mode as an off-grid sample of a deformation vector field. Predictions of deformability are compared with experimental data in the form of dihedral angle differences between two conformations of ten kinases by using a modified correlation function. Deformability calculations correlate well with experimental results and validate the applicability of this method to protein flexibility predictions.
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