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- W2054746078 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." @default.
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- W2054746078 date "2014-06-01" @default.
- W2054746078 modified "2023-10-14" @default.
- W2054746078 title "Rigidity, Secondary Structure, and the Universality of the Boson Peak in Proteins" @default.
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- W2054746078 doi "https://doi.org/10.1016/j.bpj.2014.05.009" @default.
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