英文リライト見本（イギリス英語）
英文リライト（イギリス英語）の見本です。
リライトは校正と異なり変更が多いので、実際は「履歴なしのみ」の納品となります。
（履歴つきファイルは納品いたしません）
EDIT LEVEL THREE
リライトの工程は下記のようになります。
BarThe bar-headed goose, Anser indicus, has markedly higher has a lot oftolerance for low oxygen pressures than related lowland species, such as the greylag goose, A. anser [Note: inconsistent use of Latin species name]. contrary to A. anser This increased tolerance is reflected in the significantly higher and high hemoglobin oxygen affinity of its haemoglobin (Hb) [Note: UK spelling & definition of abbreviation on first use], which allows this species to it to survive at higher altitudes than its lowland relatives. .
The Hbs of these two species show There are only four amino acid differences in the Hb of these species, but . However, a substitution Pro for to Ala substitution [Note: ambiguous-PDB check indicates Pro→Ala not Ala→Pro] at amino acid residue 119 in bar-headed goose Hb makes smaller reduces contact between the α1 subunit and β1 subunits in compared comparison to with A. anser. , The which confers enlarged increased oxygen affinity is due to by destabilization destabilising [Note: UK spelling] the protein’s deoxy T state of the protein due to lessening as a result of relaxation of the α1β1 interface. In this paper t The crystal structure of A. indicus oxy-haemoglobin [Note: UK spelling] was solved by he A. indicus oxy-hemoglobin crystal structure is found out using X-ray diffraction at a 2 Å resolution of 2 Å (PDB entry: 1a4f) and we is described here it in compared comparison to with the deoxy T state (PDB entry: 1hv4).
Overall, the In general bar-headed goose haemoglobin molecule shows the has same general structure as other Hb Hbs, and is consisting of a tetramer made of two 141 residue α-chains and two 146 residue β-chains of 141 and 146 residues, respectively, noncovalently bound with to each other noncovalently. almost The molecule is comprised primarily of antiparallel helix helices (almostly α-helixhelices) tied to little linked by short β-turns without with 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, Anser indicus, has markedly higher tolerance for low oxygen pressures than related lowland species, such as the greylag goose, A. anser [Note: inconsistent use of Latin species name]. This increased tolerance is reflected in the significantly higher oxygen affinity of its haemoglobin (Hb) [Note: UK spelling & definition of abbreviation on first use], which allows this species to survive at higher altitudes than its lowland relatives.
The Hbs of these two species show only four amino acid differences. However, a Pro to Ala substitution [Note: ambiguous-PDB check indicates Pro→Ala not Ala→Pro] at amino acid residue 119 in bar-headed goose Hb reduces contact between the α1 and β1 subunits in comparison with A. anser, which confers increased oxygen affinity by destabilising [Note: UK spelling] the deoxy T state of the protein as a result of relaxation of the α1β1 interface. The crystal structure of A. indicus oxy-haemoglobin [Note: UK spelling] was solved by X-ray diffraction at a resolution of 2 Å (PDB entry: 1a4f) and is described here in comparison with the deoxy T state (PDB entry: 1hv4).
Overall, the bar-headed goose haemoglobin molecule shows the same general structure as other Hbs, consisting of a tetramer of two α- and two β-chains of 141 and 146 residues, respectively, bound to each other noncovalently. The molecule is comprised primarily of antiparallel helices (mostly α-helices) linked by short β-turns with no β-sheets.
