Journal Article

IMPULSE-2026-00038

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Modulation of Protein Dynamics by Glycerol in Water-Soluble Chlorophyll-Binding Protein (WSCP)

Hajizadeh, M. ; Golub, M. ; Bektas, I. ; Rusevich, L. L. ; Embs, J. P. ; Lohstroh, W.MLZ* ; Paulsen, H. ; Pieper, J. (Corresponding author)

2025
MDPI Basel

Please use a persistent id in citations: doi:10.3390/cryst15060569

Abstract: Proteins are inherently dynamic entities that rely on flexibility across multiple timescales to perform their biological functions. The surrounding environment plays a critical role in modulating protein dynamics by exerting plasticizing or stabilizing effects. In order to characterize the conformational dynamics of Water-Soluble Chlorophyll-Binding Protein (WSCP), we measured Quasielastic Neutron Scattering (QENS) spectra over a wide temperature range between 100 and 300 K. The impact of glycerol, a common stabilizer, is investigated by comparing WSCP dissolved in a glycerol–water-containing buffer (WSCPW+G) with WSCP in a water-containing buffer (WSCPW). The results indicate that conformational protein dynamics are widely suppressed below 200 K but increase above this threshold, with the appearance of localized protein motions on the picosecond timescale. Glycerol appears to limit protein mobility between 280 and 300 K due to its high viscosity and hydrogen bonding in contrast to WSCP in water. Inelastic Neutron Scattering (INS) reveals the vibrational dynamics of WSCP with pronounced low-energy protein vibrations observed at about 2.5 and 6 meV. In the presence of glycerol, however, a stiffening of the vibrational motions which shifts the vibrational peaks to higher frequencies is observed.

Keyword(s): Polymers, Soft Nano Particles and Proteins (1st) ; Biology (2nd) ; Soft Condensed Matter (2nd)

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Contributing Institute(s):

1. TOFTOF (TOFTOF)

Experiment(s):

1. TOFTOF: Cold neutron time-of-flight spectrometer (NL2au)

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