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