Effective rotational correlation times of proteins from NMR relaxation interference |
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| Authors: | Lee Donghan Hilty Christian Wider Gerhard Wüthrich Kurt |
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| Institution: | 1. Bioorganic Research Institute, Suntory Foundation for Life Sciences, 1-1-1 Wakayamadai, Shimamoto, Mishima, Osaka 618-8503, Japan;2. Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan;3. Department of Structural and Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA;4. Department of Life and Coordination-Complex Molecular Science, Biomolecular Functions, Institute of Molecular Science, National Institute of Natural Sciences, Japan;5. Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-Ku, Kyoto 615-8510, Japan;1. Department of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot 7610001, Israel;2. Department of Physics, Indian Institute of Space Science and Technology, Valiamala, Thiruvananthapuram 695 547, Kerala, India;3. Nicolae Titulescu nr. 8, Turda, Jud. Cluj, Romania;4. School of Chemistry, University of Southampton, Southampton SO17 1BJ, UK |
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| Abstract: | Knowledge of the effective rotational correlation times, tauc, for the modulation of anisotropic spin-spin interactions in macromolecules subject to Brownian motion in solution is of key interest for the practice of NMR spectroscopy in structural biology. The value of tauc enables an estimate of the NMR spin relaxation rates, and indicates possible aggregation of the macromolecular species. This paper reports a novel NMR pulse scheme, 15N,1H]-TRACT, which is based on transverse relaxation-optimized spectroscopy and permits to determine tauc for 15N-1H bonds without interference from dipole-dipole coupling of the amide proton with remote protons. 15N,1H]-TRACT is highly efficient since only a series of one-dimensional NMR spectra need to be recorded. Its use is suggested for a quick estimate of the rotational correlation time, to monitor sample quality and to determine optimal parameters for complex multidimensional NMR experiments. Practical applications are illustrated with the 110 kDa 7,8-dihydroneopterin aldolase from Staphylococcus aureus, the uniformly 15N-labeled Escherichia coli outer membrane protein X (OmpX) in 60 kDa mixed OmpX/DHPC micelles with approximately 90 molecules of unlabeled 1,2-dihexanoyl-sn-glycero-3-phosphocholine (DHPC), and the 16 kDa pheromone-binding protein from Bombyx mori, which cover a wide range of correlation times. |
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