C-13 chemical shift tensor of L-tryptophan and its application to polypeptide structure determination
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Optimal Isotope Labeling of Aromatic Amino Acid Side Chains for NMR Studies of Protein Dynamics
2019, Methods in EnzymologyCitation Excerpt :For instance R1 values of Fɛ in GB1 are higher than R1 values of Yɛ, while {1H–}13C NOE values are comparable (Fig. 6), except for the more flexible surface-exposed Y33. CSA values derived from solid-state NMR of the free amino acids (Separovic, Ashida, Woolf, Smith, & Terao, 1999; Separovic, Hayamizu, Smith, & Cornell, 1991; Ye, Fu, Hu, Hou, & Ding, 1993) allow for a more appropriate use of CSA values of individual positions model-free analysis and for somewhat realistic propagation of uncertainties to the order parameter. However, what we know of CSA values of aromatic side chain 13C is far less established than for amide 15N, and therefore having an impact on the precise determination of order parameters at the moment.
Ion channel stability of Gramicidin A in lipid bilayers: Effect of hydrophobic mismatch
2014, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :NMR study has shown that in sodium dodecyl sulphate (SDS) micelle Trp-9 and Trp-15 do not interact through space [71] while in DMPC bilayer they are stacked [72]. In previous experimental studies tryptophan orientation in membrane was determined and it was shown that the indole ring is oriented parallel with the channel axis [73,74]. In addition, the presence of aromatic interaction in membrane on a nanosecond timescale has been proved [75].
NMR Studies of Ion-transporting Biological Channels
1999, Annual Reports on NMR SpectroscopyDesign and characterization of gramicidin channels
1999, Methods in EnzymologyDNA Duplex Dynamics: NMR Relaxation Studies of a Decamer with Uniformly <sup>13</sup>C-Labeled Purine Nucleotides
1998, Journal of Magnetic Resonance