PROTAMINES .2. CIRCULAR-DICHROISM STUDY OF THE 3 MAIN COMPONENTS OF CLUPEINE

被引:27
作者
TONIOLO, C
BONORA, GM
MARCHIORI, F
BORIN, G
FILIPPI, B
机构
[1] Centro di Studi sui Biopolimeri, C.N.R., Instituto di Chimica Organica, 35100 Padova
关键词
Circular dichroism; Clupeine; Peptide conformation; Protamine; α-Helix;
D O I
10.1016/0005-2795(79)90418-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The three main components YI, YII, and Z of clupeine, a protamine from herring, have been purified and characterized. The conformational preferences of clupeines have been examined as a function of pH, temperature, added salts, and presence of structure-disrupting agents and helix-supporting solvents using circular dichroism. It was found that these small basic proteins assume predominantly an unordered conformation in aqueous solution. Addition of counter ions, in particular perchlorate, and 2-chloroethanol induces in various amounts the onset of the right-handed α-helical conformation. Urea favors the statistical coil state. It was also demonstrated that in the 0.1-4.0 · 10-1 M range, in contrast to clupeines YI and Z, the circular dichroic properties of the YII component do not seem to be sensitive to the addition of mono- and diphosphate. © 1979.
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页码:429 / 439
页数:11
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