Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures
Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures
Xu YiKeith J. FritzschingRivkah RogawskiYunyao XuAnn E. McDermottaDepartment of Chemistry, Columbia University, New York, NY 1002...
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Proceedings of the National Academy of Sciences, Volume 121, Issue 8, February 2024.
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[NMR paper] Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures
Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures
While low-temperature Nuclear Magnetic Resonance (NMR) holds great promise for the analysis of unstable samples and for sensitizing NMR detection, spectral broadening in frozen protein samples is a common experimental challenge. One hypothesis explaining the additional linewidth is that a variety of conformations are in rapid equilibrium at room temperature and become frozen, creating an inhomogeneous distribution at cryogenic temperatures. Here, we investigate conformational heterogeneity...
[NMR paper] Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures
Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures
While low temperature NMR holds great promise for the analysis of unstable samples and for sensitizing NMR detection, spectral broadening in frozen protein samples is a common experimental challenge. One hypothesis explaining the additional linewidth is that a variety of conformations are in rapid equilibrium at room temperature and become frozen, creating an inhomogeneous distribution at cryogenic temperatures. Here we investigate conformational heterogeneity by measuring the backbone...
[NMR paper] NMR Elucidation of Monomer-dimer transition and Conformational heterogeneity in Histone-like DNA binding protein of Helicobacter pylori (Hup).
NMR Elucidation of Monomer-dimer transition and Conformational heterogeneity in Histone-like DNA binding protein of Helicobacter pylori (Hup).
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Authors: Jaiswal N, Raikwal N, Pandey H, Agarwal N, Arora A, Poluri KM, Kumar D
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[NMR paper] NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformation
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J Biol Chem. 2004 Aug 13;279(33):34963-70
Authors: Santiveri CM, Pérez-Cañadillas JM, Vadivelu MK, Allen MD, Rutherford TJ, Watkins NA, Bycroft M
The structure of alpha-hemoglobin stabilizing protein (AHSP), a molecular chaperone for free alpha-hemoglobin, has been determined using NMR spectroscopy....