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The Bbar-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 . These characteristics, which   allows allow 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.

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. These characteristics allow 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.

The Bbar-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 anser [Note: inconsistent use of Latin species name; also the full genus name is usually required on first use for each species]. 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 as a result ofdue to 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 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 possessing 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.

The bar-headed goose, Anser indicus, has markedly higher tolerance for low oxygen pressures than related lowland species, such as the greylag goose, Anser anser [Note: inconsistent use of Latin species name; also the full genus name is usually required on first use for each species]. 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 protein's deoxy T state due to 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, and is a tetramer possessing 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.