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• W635642784 abstract "Determining the internal motions of a protein on nanosecond-to-microsecond timescales and on nanometer length scales is challenging by experimental biophysical techniques. Neutron spin echo spectroscopy (NSE) offers a unique opportunity to determine such nanoscale protein domain motions. However, the major hurdle in applying NSE to determine nanoscale protein motion is that the time and length scales of internal protein motions tend to be comparable to that of the global motions of a protein. The signals detected by NSE tend to be dominated by rigid-body translational and rotational diffusion. Using theoretical analyses, our laboratory showed that selective deuteration of a protein domain or a subunit can enhance the capability of NSE to reveal the internal motions in a protein complex. Here, we discuss the essential theoretical analysis and experimental methodology in detail. Protein nanomachines are far more complex than any molecular motors that have been artificially constructed, and their skillful utilization likely represents the future of medicine. With selective deuteration, NSE will allow us to see these nanomachines in motion." @default.
• W635642784 created "2016-06-24" @default.
• W635642784 creator A5018868348 @default.
• W635642784 creator A5078952328 @default.
• W635642784 date "2016-01-01" @default.
• W635642784 modified "2023-10-10" @default.
• W635642784 title "Essential Strategies for Revealing Nanoscale Protein Dynamics by Neutron Spin Echo Spectroscopy" @default.
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• W635642784 doi "https://doi.org/10.1016/bs.mie.2015.05.011" @default.
• W635642784 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26791982" @default.
• W635642784 hasPublicationYear "2016" @default.
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