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[求助]
求助一段英文资料的翻译！谢谢~
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The overall structure of aromatase The structure of aromatase consists of 12 major α-helices (A to L) and 10 β-strands (1 to 10) distributed into one major and three minor sheets, and follows the characteristic cytochrome P450 fold (Fig. 1a). The major β-sheet is a mixed four-stranded sheet that begins near the N terminus (β1:83–88 and β2:93–97) but ends in two strands from the C-terminal half of the polypeptide chain (β3:373–376 and β6:393–396). The N-terminal residues 47–50 make one backbone hydrogen bond with β1 and add an extra β-strand-like element to this sheet in aromatase. Each of the three minor sheets consists of two antiparallel strands scattered over the polypeptide chain (sheet2: β4:381–383 and β5:386–388; sheet3: β8:473–475 and β9:479–481; sheet4: β7:458–461 and β10:491–494). Of the 12 major helices, I (293–324), F (210–227), G (242–267), H (278–287), C (138–152), D (155–174), E (187–205), J (326–341), K (354–366) and L (440–455) are similar to those found in most of the cytochrome P450s. Helices A′ (57–68), A (69–80), B′ (100–109), B (119–126), G′ (232–236), H′ (271– 274), J′ (346–349), K′ (398–404) and K″ (414–418) are one to four turns long and have more variability among P450s. The residues in aromatase involved in haem coordination are Arg 115, Trp 141, Arg 145, Arg 375 and Arg 435. 由于生物基础差，术语都不了解，还请各位专业人士帮忙，谢谢各位~  1.jpg  2.jpg |
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2楼2015-12-07 09:35:57
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