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??Ď? 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 and Tyr in the aromatic cluster in GB1. We found that all four residues of the cluster, Y3, F30, Y45 and F52, display slow ring flips. Interestingly, F52, the central residue of the cluster, which makes aromatic contacts with all three others, is flipping significantly faster, while the other rings are flipping with the same rates within margin of error. Determined activation enthalpies and activation volumes of these processes are in the same range of other reported ring flips of single aromatic rings. There is no correlation of the number of aromatic stacking interactions to the activation enthalpy, and no correlation of the ringâ??s extent of burying to the activation volume. Because of these findings, we speculate that F52 is undergoing concerted ring flips with each of the other rings.
Conformational exchange of aromatic side chains by 1 H CPMG relaxation dispersion
Conformational exchange of aromatic side chains by 1 H CPMG relaxation dispersion
Abstract
Aromatic side chains are attractive probes of protein dynamics on the millisecond time scale, because they are often key residues in enzyme active sites and protein binding sites. Further they allow to study specific processes, like histidine tautomerization and ring flips. Till now such processes have been studied by aromatic 13C CPMG relaxation dispersion experiments. Here we investigate the possibility of aromatic 1H CPMG relaxation dispersion experiments...
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11-25-2018 06:02 AM
Engineering Aromatic–Aromatic InteractionsTo Nucleate Folding in Intrinsically Disordered Regions of Proteins
Engineering Aromatic–Aromatic InteractionsTo Nucleate Folding in Intrinsically Disordered Regions of Proteins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00437/20170810/images/medium/bi-2017-00437t_0014.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00437
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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08-11-2017 08:52 PM
Off-resonance rotating-frame relaxation dispersion experiment for 13C in aromatic side chains using L-optimized TROSY-selection
Off-resonance rotating-frame relaxation dispersion experiment for 13C in aromatic side chains using L-optimized TROSY-selection
Abstract
Protein dynamics on the microsecondâ??millisecond time scales often play a critical role in biological function. NMR relaxation dispersion experiments are powerful approaches for investigating biologically relevant dynamics with site-specific resolution, as shown by a growing number of publications on enzyme catalysis, protein folding, ligand binding, and allostery. To date, the majority of studies has probed the...
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06-19-2014 10:21 PM
[NMR paper] Slow Aromatic Ring Flips Detected Despite Near-Degenerate NMR Frequencies of the Exchanging Nuclei.
Slow Aromatic Ring Flips Detected Despite Near-Degenerate NMR Frequencies of the Exchanging Nuclei.
Related Articles Slow Aromatic Ring Flips Detected Despite Near-Degenerate NMR Frequencies of the Exchanging Nuclei.
J Phys Chem B. 2013 Jul 16;
Authors: Weininger U, Respondek M, Löw C, Akke M
Abstract
Aromatic ring flips of Phe and Tyr residues are a hallmark of protein dynamics with a long history in molecular biophysics. Ring flips lead to symmetric exchange of nuclei between sites with distinct magnetic environments, which can be...
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07-19-2013 09:20 PM
Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected 13C CPMG relaxation dispersion
Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected 13C CPMG relaxation dispersion
Abstract Protein dynamics on the millisecond time scale commonly reflect conformational transitions between distinct functional states. NMR relaxation dispersion experiments have provided important insights into biologically relevant dynamics with site-specific resolution, primarily targeting the protein backbone and methyl-bearing side chains. Aromatic side chains represent attractive probes of protein dynamics because they are over-represented in protein binding...
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07-30-2012 07:42 AM
[NMR paper] NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins.
NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins.
Related Articles NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins.
J Am Chem Soc. 2005 Sep 14;127(36):12620-6
Authors: Torizawa T, Ono AM, Terauchi T, Kainosho M
The unambiguous assignment of the aromatic ring resonances in proteins has been severely hampered by the inherently poor sensitivities of the currently available methodologies developed for uniformly 13C/15N-labeled...
Slow ring flips in aromatic cluster of GB1 studied by aromatic 13 C relaxation dispersion methods
Linear Mode
