Abstract
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 β-strands contribute greater than two-thirds of the intensity to the low-frequency vibrational spectra of GFP.
Original language | English |
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Pages (from-to) | 2182-2187 |
Number of pages | 6 |
Journal | Biophysical Journal |
Volume | 105 |
Issue number | 9 |
DOIs | |
State | Published - Nov 5 2013 |
Funding
J.D.N. and A.P.S. acknowledge Department of Energy support through the Experimental Program to Stimulate Competitive Research (grant No. DE-FG02-08ER46528). H.O’N. and Q.Z. acknowledge the support of the Center for Structural Molecular Biology at Oak Ridge National Laboratory, supported by the Department of Energy Office of Science, Office of Biological and Environmental Research Project No. ERKP291. The research at the Spallation Neutron Source was sponsored by the Scientific User Facilities Division, Department of Energy Office of Basic Energy Sciences.
Funders | Funder number |
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Department of Energy Office of Basic Energy Sciences | |
Office of Biological and Environmental Research Project | ERKP291 |
U.S. Department of Energy | DE-FG02-08ER46528 |