Solution structure of a D,L-alternating oligonorleucine as a model of double-stranded antiparallel β-helix
✍ Scribed by E. Navarro; E. Fenude; B. Celda
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2002
- Tongue
- English
- Weight
- 846 KB
- Volume
- 64
- Category
- Article
- ISSN
- 0006-3525
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📜 SIMILAR VOLUMES
## Abstract Alternating sequences of D and L residues in peptides are directly related to the formation of several kinds of regular helical conformations usually called β‐helices. The major feature of these structures is that they can be associated with the transmembrane ion‐conducting channel acti
The structure of Boc-(L-Val-D-Val),-OMe has been determined by x-ray single-crystal diffraction analysis. The octapepti+ crystallizes in the trigonal system, space group P3,21 with a = b = 12.760 A, c = 63.190 A and Z = 6. The independent unit is represented by one octapeptide chain. The structure h
The crystal structure of Boc-(L-Phe-D-Phe),-OMe has been determined by x-ray diffracti2n analysis. peptide cry@llizes in the triclinic system, space group P1 with a = 15.290 A, b = 15.163 A, c = 19.789 A, a = 102.49', 8 = 96.59", y = 74.22", and Z = 2. The structure has been solved by coupling of t
## Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable v