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??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...
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02-29-2020 09:52 PM
[NMR paper] Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations.
Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations.
Related Articles Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations.
Phys Chem Chem Phys. 2015 Oct 9;
Authors: Paluch P, Pawlak T, Jeziorna A, Trébosc J, Hou G, Vega AJ, Amoureux JP, Dracinsky M, Polenova T, Potrzebowski MJ
Abstract
We report a new multidimensional magic angle spinning...
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10-10-2015 06:47 PM
[NMR paper] Nature of aryl-tyrosine interactions contribute to ?-hairpin scaffold stability: NMR evidence for alternate ring geometry.
Nature of aryl-tyrosine interactions contribute to ?-hairpin scaffold stability: NMR evidence for alternate ring geometry.
Nature of aryl-tyrosine interactions contribute to ?-hairpin scaffold stability: NMR evidence for alternate ring geometry.
Phys Chem Chem Phys. 2015 Jan 8;
Authors: Makwana KM, Mahalakshmi R
Abstract
The specific contribution of the acidic-aromatic ?-sheet favouring amino acid tyrosine to the stability of short octapeptide ?-hairpin structures is presented here. Solution NMR analysis in near-apolar...
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01-09-2015 03:58 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
[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...
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12-01-2010 06:56 PM
[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...