Measurement of SDS Micelle-Peptide Association Using (1)H NMR Chemical Shift Analysis and Pulsed-Field Gradient NMR Spectroscopy.

@article{Orfi1998MeasurementOS,
  title={Measurement of SDS Micelle-Peptide Association Using (1)H NMR Chemical Shift Analysis and Pulsed-Field Gradient NMR Spectroscopy.},
  author={L Orfi and Min Y. Lin and Cynthia K Larive},
  journal={Analytical chemistry},
  year={1998},
  volume={70 7},
  pages={1339-45}
}
The binding of two simple tripeptides, glycyl-histidyl-glycine (GHG) and phenylalanyl-histidyl-phenylalanine (FHF) with SDS micelles was examined using (1)H NMR chemical shift analysis and self-diffusion coefficients measured with pulsed-field gradient NMR spectroscopy. The presence of GHG or FHF did not appear to significantly affect the critical micelle concentration (cmc) or the average size of the SDS micelles formed. The chemical shifts of several of the GHG resonances change as a function… CONTINUE READING