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A ProtonT1,T2, and NOE Study of Relative Motion of the Indole Ring of Tryptophans in Gramicidin Analogs Incorporated into SDS Micelles
Authors:JF Hinton  AM Washburn-McCain
Institution:Department of Chemistry/Biochemistry, University of Arkansas, Fayetteville, Arkansas, 72701
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.
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