Site-Selective Dynamics of Ligand-Free and Ligand-Bound Azidolysozyme

Salehi, Seyedeh Maryam and Meuwly, Markus. (2022) Site-Selective Dynamics of Ligand-Free and Ligand-Bound Azidolysozyme. Journal of Clinical Physics, 156. p. 105105.

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Azido-modified alanine residues (AlaN3) are environment-sensitive, minimally invasive infrared probes for the site-specific investigation of protein structure and dynamics. Here, the capability of the label is investigated to query whether or not a ligand is bound to the active site of lysozyme and how the spectroscopy and dynamics change upon ligand binding. The results demonstrate specific differences for center frequencies of the asymmetric azide stretch vibration, the longtime decay, and the static offset of the frequency fluctuation correlation function (FFCF)—all of which are experimental observables—between the ligand-free and the ligand-bound N3-labeled protein. The center-frequency shifts range from 1 to 8 cm−1, which is detectable from state-of-the art experiments. Similarly, the nonvanishing static component Δ0 of the FFCF between ligand-free and ligand-bound protein can differ by up to a factor of 2.5. This makes the azide label a versatile and structurally sensitive probe to report on the dynamics of proteins in a variety of environments and for a range of different applications. Ligand-induced differences in the dynamics are also mapped onto changes in the local and through-space coupling between residues by virtue of dynamical cross correlation maps. This demonstrates that the position where the label is placed also influences the local and global protein motions.
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie > Physikalische Chemie (Meuwly)
UniBasel Contributors:Meuwly, Markus
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Institute of Physics
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:16 Feb 2023 09:34
Deposited On:16 Feb 2023 09:34

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