Affiliation:
1. Department of Chemistry, University of Basel, Klingelbergstrasse 80, CH-4056 Basel, Switzerland
Abstract
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.
Funder
Swiss National Science Foundation
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Cited by
2 articles.
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1. Biomolecular dynamics in the 21st century;Biochimica et Biophysica Acta (BBA) - General Subjects;2024-02
2. Special issue on time-resolved vibrational spectroscopy;The Journal of Chemical Physics;2023-04-28