[NMR paper] NMR Studies of Aromatic Ring Flips to Probe Conformational Fluctuations in Proteins
NMR Studies of Aromatic Ring Flips to Probe Conformational Fluctuations in Proteins
Aromatic residues form a significant part of the protein core, where they make tight interactions with multiple surrounding side chains. Despite the dense packing of internal side chains, the aromatic rings of phenylalanine and tyrosine residues undergo 180° rotations, or flips, which are mediated by transient and large-scale "breathing" motions that generate sufficient void volume around the aromatic ring. Forty years after the seminal work by Wagner and Wüthrich, NMR studies of aromatic ring...
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[NMR paper] Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD
Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD
Probing the dynamics of aromatic side chains provides important insights into the behavior of a protein because flips of aromatic rings in a protein's hydrophobic core report on breathing motion involving a large part of the protein. Inherently invisible to crystallography, aromatic motions have been primarily studied by solution NMR. The question how packing of proteins in crystals affects ring flips has, thus, remained largely unexplored. Here we apply magic-angle spinning NMR, advanced...
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Slow ring flips in aromatic cluster of GB1 studied by aromatic 13 C relaxation dispersion methods
Slow ring flips in aromatic cluster of GB1 studied by aromatic 13 C relaxation dispersion methods
Abstract
Ring flips of phenylalanine and tyrosine are a hallmark of protein dynamics. They report on transient breathing motions of proteins. In addition, flip rates also depend on stabilizing interactions in the ground state, like aromatic stacking or cationâ??Ï? interaction. So far, experimental studies of ring flips have almost exclusively been performed on aromatic rings without stabilizing interactions. Here we investigate ring flip dynamics of Phe...
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[NMR paper] Aromatic ring-flipping in supercooled water: implications for NMR-based structural bi
Aromatic ring-flipping in supercooled water: implications for NMR-based structural biology of proteins.
Related Articles Aromatic ring-flipping in supercooled water: implications for NMR-based structural biology of proteins.
J Am Chem Soc. 2001 Jan 24;123(3):388-97
Authors: Skalicky JJ, Mills JL, Sharma S, Szyperski T
We have characterized, for the first time, motional modes of a protein dissolved in supercooled water: the flipping kinetics of phenylalanyl and tyrosinyl rings of the 6 kDa protein BPTI have been investigated by NMR at...
Visualizing protein breathing motions associated with aromatic ring flipping - Nature.com
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