Journal
BIOPHYSICAL JOURNAL
Volume 105, Issue 9, Pages 2182-2187Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2013.09.029
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Funding
- Department of Energy [DE-FG02-08ER46528]
- Center for Structural Molecular Biology at Oak Ridge National Laboratory
- Department of Energy Office of Science, Office of Biological and Environmental Research Project [ERKP291]
- Scientific User Facilities Division, Department of Energy Office of Basic Energy Sciences
- U.S. Department of Energy (DOE) [DE-FG02-08ER46528] Funding Source: U.S. Department of Energy (DOE)
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Collective dynamics are considered to be one of the major properties of soft materials, including biological macromolecules. We present coherent neutron scattering studies of the low-frequency vibrations, the so-called boson peak, in fully deuterated green fluorescent protein (GFP). Our analysis revealed unexpectedly low coherence of the atomic motions in GFP. This result implies a low amount of in-phase collective motion of the secondary structural units contributing to the boson peak vibrations and fast conformational fluctuations on the picosecond timescale. These observations are in contrast to earlier studies of polymers and glass-forming systems, and suggest that random or out-of-phase motions of the beta-strands contribute greater than two-thirds of the intensity to the low-frequency vibrational spectra of GFP.
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