Chen R, Krämer C, Schmidmayr W, Henning U
Proc Natl Acad Sci U S A. 1979 Oct;76(10):5014-7. doi: 10.1073/pnas.76.10.5014.
The amino acid sequence of the pore-forming outer membrane protein I (porin) from Escherichia coli B/r has been determined. The polypeptide contains 340 amino acid residues resulting in a molecular weight of 37,205. The transmembrane polypeptide has no stretches of nonpolar residues, uninterrupted by charged side chains, longer than 11 amino acid residues. Regarding polarity, the chain can be subdivided into three regions: a distinctly hydrophilic region between residues 1 and 82 (51.2% polarity), a fairly nonpolar region between residues 83 and 194 (33.9% polarity), and a more hydrophilic region up to the COOH terminus (48% polarity). These results are interpreted as evidence against a simple transmembrane structure in which the membrane is spanned by a single contiguous sequence of hydrophobic amino acids, as has been proposed, for example, for glycophorin.
已确定来自大肠杆菌B/r的成孔外膜蛋白I(孔蛋白)的氨基酸序列。该多肽含有340个氨基酸残基,分子量为37,205。跨膜多肽没有不被带电侧链打断的、长度超过11个氨基酸残基的非极性残基片段。就极性而言,该链可分为三个区域:残基1至82之间明显亲水的区域(极性为51.2%)、残基83至194之间相当非极性的区域(极性为33.9%)以及直至COOH末端的更亲水区域(极性为48%)。这些结果被解释为反对一种简单跨膜结构的证据,在这种结构中,膜由单一连续的疏水氨基酸序列跨越,例如对血型糖蛋白所提出的那样。