X-ray diffraction studies of certain lipide-protein complexes
β Scribed by Palmer, Kenneth J. ;Schmitt, Francis O. ;Chargaff, Erwin
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1941
- Tongue
- English
- Weight
- 324 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0095-9898
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β¦ Synopsis
Cephalin readily combines with basic proteins, such as histones, forming a precipitate which may be insoluble in water and organic solvents (Chargaff, '38; Chargaff and Ziff, '39). From the combining ratios it was shown that cephalin, which is acidic, combines with basic proteins through salt linkages with the basic terminal amino groups of the protein side chains. Lecithin shows similar properties only at those p H levels ( > 7 ) where the molecules are negatively charged, and these
π SIMILAR VOLUMES
Polyaniline (PAn), a n important conducting polymer, was synthesized chemically. Percentage crystallinity of' PAn on doping with various dopants (viz., hydrochloric acid, formic acid, iodine, methylene blue) has been investigated using wide-angle X-ray diffraction analysis. It is observed that perce