Protein architecture and the origin of introns.
Protein architecture and the origin of introns.
复制标题
蛋白质结构和内含子的起源。
DOI:
10.1101/sqb.1987.052.01.100
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发表时间:
1987
期刊:
影响因子:
--
通讯作者:
M. Nosaka
中科院分区:
文献类型:
--
作者:
M. Go;M. Nosaka
METHODModules introduced originally are segments defined by partitioning a globular domain into relatively compact regions consisting of about 20-40 contiguous amino acid residues (G6 1981). The algorithm was applied to a small protein such as lysozyme (G6 1983) and cytochrome c (G6 1985), a small domain such as ovomucoid third domain (G5 1985), and a small subunit, hemoglobin a and/3 chains (G5 1981). In these monolayer domains or subunits having no core modules buried inside, the joints of the modules are characterized by their locations not being close to the surface of the domains or subunits (G6 1981). Utilization of this characteristic as well as the compactness itself makes easier the identification of modules in a small domain or subunit consisting of monolayer modules; the modules can be identified by the fact that their joints are located not far from all the other residues. Search for such joints was carried out by using a distance map on which amino acid residues separated from each other by more than a certain distance were marked.