A ProtonT1,T2, and NOE Study of Relative Motion of the Indole Ring of Tryptophans in Gramicidin Analogs Incorporated into SDS Micelles

@inproceedings{Hinton1997APA,
  title={A ProtonT1,T2, and NOE Study of Relative Motion of the Indole Ring of Tryptophans in Gramicidin Analogs Incorporated into SDS Micelles},
  author={James F. Hinton and A. M. Washburn-McCain},
  year={1997}
}
Abstract The proton spin–lattice relaxation time, spin–spin relaxation time, and NOE of the indole ring NH proton of tryptophan residues have been determined for seven analogs of gramicidin A incorporated into SDS micelles. The data obtained indicate that the motion of the indole rings systematically decreases, proceeding from the aqueous interface to the interior of the micelle.