Time-resolved protein side-chain motions unraveled by high-resolution relaxometry and molecular dynamics simulations

Abstract : Motions of proteins are essential for the performance of their functions. Aliphatic protein side chains and their motions play critical roles in protein interactions: for recognition and binding of partner molecules at the surface or serving as an en-tropy reservoir within the hydrophobic core. Here, we present a new NMR method based on high-resolution relaxometry and high-field relaxation to determine quantitatively both motional amplitudes and timescales of methyl-bearing side chains in the picose-cond-to-nanosecond range. We detect a wide variety of motions in isoleucine side chains in the protein ubiquitin. We unambiguous-ly identify slow motions in the low nanosecond range, which, in conjunction with molecular dynamics computer simulations, could be assigned to transitions between rotamers. Our approach provides unmatched detailed insight into the motions of aliphatic side chains in proteins and provides a better understanding of the nature and functional role of protein side-chain motions.
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Submitted on : Thursday, November 15, 2018 - 2:40:34 PM
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Samuel Cousin, Pavel Kadeřávek, Nicolas Bolik-­coulon, Yina Gu, Cyril Charlier, et al.. Time-resolved protein side-chain motions unraveled by high-resolution relaxometry and molecular dynamics simulations. Journal of the American Chemical Society, American Chemical Society, 2019. ⟨hal-01923807⟩

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