## Abstract The three‐dimensional structure of a cyclic bouvardin analogue, cyclo (‐Pro‐MeTyr‐Ala‐MeTyr‐MeTyr‐D‐Ala‐) has been determined by distance geomtry calculation and restrained energy minimization from nmr data. The preparation of the input for the distance geometry calculations, the modifi
Solution three-dimensional structure of surfactin: A cyclic lipopeptide studied by 1H-nmr, distance geometry, and molecular dynamics
✍ Scribed by Jean-Marc Bonmatin; Monique Genest; Henri Labbé; Marius Ptak
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1994
- Tongue
- English
- Weight
- 878 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0006-3525
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The cis/trans conformational equilibrium of the two Ac-Pro isomers of the beta-turn model dipeptide [13C]-Ac-L-Pro-D-Ala-NHMe, 98% 13C enriched at the acetyl carbonyl atom, was investigated by the use of variable temperature gradient enhanced 1H-nmr, two-dimensional (2D) 1H,1H nuclear Overhauser eff