Experimental mapping of short-wavelength phonons in proteins

Utsab R. Shrestha; Eugene Mamontov; Hugh M. O'Neill; Qiu Zhang; Alexander I. Kolesnikov; Xiangqiang Chu

doi:10.1016/j.xinn.2021.100199

Experimental mapping of short-wavelength phonons in proteins

Utsab R. Shrestha, Eugene Mamontov, Hugh M. O'Neill, Qiu Zhang, Alexander I. Kolesnikov, Xiangqiang Chu

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

Phonons are quasi-particles, observed as lattice vibrations in periodic materials, that often dampen in the presence of structural perturbations. Nevertheless, phonon-like collective excitations exist in highly complex systems, such as proteins, although the origin of such collective motions has remained elusive. Here we present a picture of temperature and hydration dependence of collective excitations in green fluorescent protein (GFP) obtained by inelastic neutron scattering. Our results provide evidence that such excitations can be used as a measure of flexibility/softness and are possibly associated with the protein's activity. Moreover, we show that the hydration water in GFP interferes with the phonon propagation pathway, enhancing the structural rigidity and stability of GFP.

Original language	English
Article number	100199
Journal	Innovation
Volume	3
Issue number	1
DOIs	https://doi.org/10.1016/j.xinn.2021.100199
State	Published - Jan 25 2022

Funding

This work was supported by NSF No. 1616008 , the Department of Energy ( DoE ), Office of Basic Energy Sciences, and Wayne State University. X.C was supported by NSAF No. U1930403 and National Natural Science Foundation of China ( NSFC ) 11875051 . Neutron scattering measurements at ORNL’s Spallation Neutron Source were supported by the Scientific User Facilities Division, Office of Basic Energy Sciences, DoE.

Keywords

collective excitations
inelastic neutron scattering
protein activity
protein dynamics

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title = "Experimental mapping of short-wavelength phonons in proteins",

abstract = "Phonons are quasi-particles, observed as lattice vibrations in periodic materials, that often dampen in the presence of structural perturbations. Nevertheless, phonon-like collective excitations exist in highly complex systems, such as proteins, although the origin of such collective motions has remained elusive. Here we present a picture of temperature and hydration dependence of collective excitations in green fluorescent protein (GFP) obtained by inelastic neutron scattering. Our results provide evidence that such excitations can be used as a measure of flexibility/softness and are possibly associated with the protein's activity. Moreover, we show that the hydration water in GFP interferes with the phonon propagation pathway, enhancing the structural rigidity and stability of GFP.",

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AU - Shrestha, Utsab R.

AU - Mamontov, Eugene

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AU - Zhang, Qiu

AU - Kolesnikov, Alexander I.

AU - Chu, Xiangqiang

PY - 2022/1/25

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AB - Phonons are quasi-particles, observed as lattice vibrations in periodic materials, that often dampen in the presence of structural perturbations. Nevertheless, phonon-like collective excitations exist in highly complex systems, such as proteins, although the origin of such collective motions has remained elusive. Here we present a picture of temperature and hydration dependence of collective excitations in green fluorescent protein (GFP) obtained by inelastic neutron scattering. Our results provide evidence that such excitations can be used as a measure of flexibility/softness and are possibly associated with the protein's activity. Moreover, we show that the hydration water in GFP interferes with the phonon propagation pathway, enhancing the structural rigidity and stability of GFP.

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Experimental mapping of short-wavelength phonons in proteins

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