## 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 diffraction study of poly-L-arginine hydrochloride
✍ Scribed by M. Suwalsky; W. Traub
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1972
- Tongue
- English
- Volume
- 11
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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 peroargiriine residue show features characterist.ic of a-helical structures including a 5.4-A layer line and a meridional 1.5-A reflection. Increasing the water content from '/z to 6'/z m:lecules p,er residue causes the a axis of the hexagon$ unit cell to increase from 14.4 A to 15.8 A, with no appreciable change in the 27.0 A c axis. Removal of the last half molecule of water results in a very diffuse pattern, but on rehydration the sharp pattern reappears.
Specimens containing five to t,wenty water molecules per residue show quite a different pattern, the spacings of Thich do not vary apprzciably with hydration. This pattern includes a meridional 3.4-A reflection, a feature commonly shown by p structures, and indeed all the re!ection.; can b t satisfactoriloy indexed in terms of a monoclinic unit cell with a = 9.26 A, b = 22.05 A, c = 6.76 A, and y = 108.9'. These dimensions are shown by models to be compatible with a B pleated-sheet structure.
📜 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
Circular dichroism (CU) measurements were carried out on various copolymers of L-tryptophan and r-ethyl L-glutamate in ethylene glycol monomethyl ether as the solvent. On increasing the L-tryptophan content of the copolymers a gradual change in the C D spectra was observed. The typical spectrum of t
## Abstract **Summary:** Solution‐grown lamellar crystals of poly(__p__‐dioxanone) (PPDX) have been crystallized isothermally from butane‐1,4‐diol at 100 °C. The crystal structure of PPDX has been determined by interpretation of X‐ray fiber diagrams of PPDX fibers and electron diffraction diagrams
## 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, a