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Alpha-helices as alignment reporters in residual dipolar coupling analysis of proteins.

J Biomol NMR

December 2024

Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892-0520, USA.

Inclusion of residual dipolar couplings (RDCs) during the early rounds of protein structure determination requires use of a floating alignment tensor or knowledge of the alignment tensor strength and rhombicity. For proteins with interdomain motion, such analysis can falsely hide the presence of domain dynamics. We demonstrate for three proteins, maltotriose-ligated maltose binding protein (MBP), Ca-ligated calmodulin, and a monomeric N-terminal deletion mutant of the SARS-CoV-2 Main Protease, MPro, that good alignment tensor estimates of their domains can be obtained from RDCs measured for residues that are identified as α-helical based on their chemical shifts.

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Background: While many clinical computed tomography (CT) protocols use helical scanning, the traditional method for measuring the volume CT Dose Index (CTDI) requires modifying the helical protocol to perform a single axial rotation. This modification can present challenges and mismatched settings across various scanner models.

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