## Abstract An X‐ray study of the synthetic polypeptide poly(L‐homoarginine hydrochloride) has been made to investigate whether, like the chemically related polypeptides poly(L‐lysine hydrochloride), poly(L‐arginine hydrochloride), and poly(L‐ornithine hydrobromide), it can undergo conformational t
An X-ray study of poly(L-prolyl-L-α-phenylglycyl-L-proline)
✍ Scribed by A. Del Pra; M. Palumbo; M. Goodman
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1976
- Tongue
- English
- Weight
- 193 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
X‐ray diffraction studies have been made on the polytripeptide poly(L‐prolyl‐L‐α‐phenylglycyl‐L‐proline). Its structure has been found to be helical, with a poly(L‐proline) II conformation, packed in an orthorhombic lattice, space group P2~1~2~1~2, with a = 14.3 Å, b = 13.5 Å, and c = 9.4 Å.
📜 SIMILAR VOLUMES
## Abstract A structural study of the synthetic polypeptide poly(L‐lysine hydrobromide) has been made by X‐ray fiber techniques. The investigation was undertaken to determine whelther this polymer undergoes conformational transitions as a function of hydration in a manner similar to other chemicall
## Abstract An X‐ray study has been made of the synthetic polypeptide poly‐L‐ornithine hydrobromide to investigate whether, like the chemically related polypeptides poly‐L‐lysine and poly‐L‐arginine hydrochlorides, it can undergo conformational changes merely from variations in its degree of hydrat
An x-ray study has been made of polyarginine hydrochloride to investigate whether, like polylysine hydrochloride, it can undergo conformational changes merely from variations in the degree of hydration. X-ray powder and fiber photographs of specimens containing up to about five molecules of water pe