A ProtonT1,T2, and NOE Study of Relative Motion of the Indole Ring of Tryptophans in Gramicidin Analogs Incorporated into SDS Micelles
✍ Scribed by J.F. Hinton; A.M. Washburn-McCain
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 246 KB
- Volume
- 125
- Category
- Article
- ISSN
- 1090-7807
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✦ Synopsis
The proton spin-lattice relaxation time, spin-spin relaxation mer channels. The two gramicidin A monomers are joined time, and NOE of the indole ring NH proton of tryptophan resiat their NH 2 termini (8-20). Single-channel conductance dues have been determined for seven analogs of gramicidin A studies have shown that there are differences in channel incorporated into SDS micelles. The data obtained indicate that properties between gramicidin A analogs formed by single the motion of the indole rings systematically decreases, proceeding amino acid substitution (21-24). Amino acid substitution from the aqueous interface to the interior of the micelle. ᭧ 1997 and side-chain orientation are thought to be important factors
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in determining the transport properties of the gramicidin channel (7,.