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X-ray diffraction studies of certain lipide-protein complexes

✍ 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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✦ 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


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X-ray diffraction study of doped polyani
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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