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Updated: Apr 28, 2026

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
Published on: April 13, 2022
Rigidity, secondary structure, and the universality of the boson peak in proteins
Stefania Perticaroli1, Jonathan D Nickels2, Georg Ehlers3
1Joint Institute for Neutron Sciences, Oak Ridge National Laboratory, Oak Ridge, Tennessee; Chemical and Materials Sciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee; Department of Chemistry, University of Tennessee, Knoxville, Tennessee.
Abstract:
Complementary neutron- and light-scattering results on nine proteins and amino acids reveal the role of rigidity and secondary structure in determining the time- and lengthscales of low-frequency collective vibrational dynamics in proteins. These dynamics manifest in a spectral feature, known as the boson peak (BP), which is common to all disordered materials. We demonstrate that BP position scales systematically with structural motifs, reflecting local rigidity: disordered proteins appear softer than α-helical proteins; which are softer than β-sheet proteins. Our analysis also reveals a universal spectral shape of the BP in proteins and amino acid mixtures; superimposable on the shape observed in typical glasses. Uniformity in the underlying physical mechanism, independent of the specific chemical composition, connects the BP vibrations to nanometer-scale heterogeneities, providing an experimental benchmark for coarse-grained simulations, structure/rigidity relationships, and engineering of proteins for novel applications.
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