期刊
BIOPHYSICAL JOURNAL
卷 106, 期 12, 页码 2667-2674出版社
CELL PRESS
DOI: 10.1016/j.bpj.2014.05.009
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资金
- Department of Energy [DE-FG02-08ER46528]
- Scientific User Facilities Division, Office of Basic Energy Sciences, U.S. Department of Energy
- UT-Battelle, LLC
- U.S. Department of Energy [DEAC05-00OR22725]
- U.S. Department of Energy (DOE) [DE-FG02-08ER46528] Funding Source: U.S. Department of Energy (DOE)
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 a-helical proteins; which are softer than beta-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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