AXIAL PACKING IN LIGHT-MEROMYOSIN PARACRYSTALS
AXIAL PACKING IN LIGHT-MEROMYOSIN PARACRYSTALS
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DOI：
10.1016/0022-2836(80)90394-0
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发表时间：
1980-01-01
影响因子：
5.6
通讯作者：
PEPE, FA
中科院分区：
文献类型：
--
作者：
SAFER, D;PEPE, FA
The positions of ends of molecules were correlated with the striation pattern in negatively stained paracrystals of light meromyosin [LMM], and the pattern of deposition of C-protein on paracrystals has been examined both in negative stain and in section. In paracrystals of papain LMM, molecules may be related by overlaps of 16 or 44 nm; in paracrystals of chymotryptic LMM, molecules may overlap by multiples of 14 nm. The polarity by which overlapping molecules are related may be deduced for those molecules which bind C-protein. In paracrystals of papain LMM, molecules may overlap by 16 nm head-to-head or by 44 nm head-to-tail; in paracrystals of chymotryptic LMM, the head-to-head and head-to-tail overlaps are 14 and 42 nm. The binding of C-protein at 42 nm intervals to paracrystals whose staining pattern shows an undifferentiated 14 nm periodicity indicates that some feature of molecular packing must repeat at 42 nm intervals. The observation of C-protein bound at the edges of paracrystals suggests that the C-protein binding site is near one end of the LMM molecule.
