校正エキスパート見本（イギリス英語）
英文校正エキスパート（イギリス英語）の見本です。
英文校正は履歴なしファイル（校正済み）と履歴付ファイル（参考資料）を納品します。
EDIT LEVEL TWO
履歴付ファイル（参考資料）は下記のようになります。
The Barbar-headed goose has a lot of higher tolerance for low oxygen pressure contrary to than A. anser and high haemoglobin (Hb) [Note: UK spelling & definition of abbreviation on first use] oxygen affinity , which allows it to survive at high altitudes. There are only four amino acid differences in the Hb of these species, but substitution of Pro for Ala [Check: “Pro with Ala” i.e. Pro->Ala vs. Ala->Pro] at position 119 in bar-headed goose Hb makes reduces smaller contact between α1 subunit and β1 subunits compared to A. anser. The enlarged increased oxygen affinity is due to destabilization destabilisation of the protein’s deoxy T- state due to lessening by relaxation of the α1β1 interface. In tThis paper describes the A. indicus oxy-haemoglobin crystal structure is found out determined using by X-ray diffraction at 2 Å resolution (PDB entry: 1a4f) and we described it in compared comparison to with the deoxy T state (PDB entry: 1hv4).
In general general, bar-headed goose haemoglobin has the same structure as other Hb Hbs, and is a tetramer comprised made of two 141 141-residue α-chains and two 146 146-residue β-chains noncovalently bound noncovalently with almost consisting mostly of antiparallel helix helices (almostly α-helixhelices) tied to little with short β-turns without and no β-sheets.
履歴なしファイル（校正済み）は下記のようになります。
The bar-headed goose has higher tolerance for low oxygen pressure than A. anser and high haemoglobin (Hb) [Note: UK spelling & definition of abbreviation on first use] oxygen affinity, which allows it to survive at high altitudes. There are only four amino acid differences in the Hb of these species, but substitution of Pro for Ala [Check: “Pro with Ala” i.e. Pro->Ala vs. Ala->Pro] at position 119 in bar-headed goose Hb reduces contact between α1 and β1 subunits compared to A. anser. The increased oxygen affinity is due to destabilisation of the protein’s deoxy T state by relaxation of the α1β1 interface. This paper describes the A. indicus oxy-haemoglobin crystal structure determined by X-ray diffraction at 2 Å resolution (PDB entry: 1a4f) in comparison with the deoxy T state (PDB entry: 1hv4).
In general, bar-headed goose haemoglobin has the same structure as other Hbs, and is a tetramer comprised of two 141-residue α-chains and two 146-residue β-chains bound noncovalently consisting mostly of antiparallel helices (mostly α-helices) with short β-turns and no β-sheets.
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