<p>Residues lining the haem distal pocket are indicated and shown in stick representation (grey). Superimposition of <i>Ma</i>Pgb*(III)-cyanide (yellow) onto (<b>A</b>) the <i>Ma</i>Pgb*(III)-cyanide Trp(60)B9Ala mutant, and (<b>B</b>) the <i>Ma</i>Pgb*(III)-cyanide Tyr(61)B10Ala mutant. The proximal His(120)F8 residue is also shown. H-bonds to the haem-Fe(III)-bound cyanide are indicated by dashed lines. The mutated residues are indicated in underlined bold characters. Both panels are shown from side and top views.</p
<p>(A) Charmm_mini; (B) Charmm_ave; (C) Charmm_706ps. In the cartoon representations, the green and ...
<p>(a) Superposition of the YW/ELA/HLA-A2 and the DMF5/ELA/HLA-A2 complexes. DMF5 α chain is yellow,...
The structural factors governing azide and cyanide binding have been examined by measuring the effec...
<p>Residues lining the haem distal pocket are indicated and shown in stick representation (grey). Su...
<p>Residues lining the heme distal pocket are indicated (one letter code) and shown in green for the...
<p>Residues lining the haem distal pocket are indicated and shown in stick representation (yellow). ...
<p>Residues lining the haem distal pocket are indicated and shown in stick representation (brown). S...
<p>Residues lining the haem distal pocket are indicated and shown in stick representation (green) fo...
<p>(Panel A) The secondary structure elements are labeled A–H’. The 20 <i>N</i>-terminal residues an...
<p>A: Cartoon representation of the PttTrHb model in cyan colour. The heme is shown as sticks colour...
<p>Residues found in contact with F476 are depicted in sticks. Three distinct hydrophobic clusters a...
Bacillus megaterium flavocytochrorne P450 BM3 (CYP102A1) is a biotechnologically important cytochrom...
<p>Amino acid residues of L35P mutant through which hydrogen bonds exert influence from the site of ...
<p>(<b>A</b>) Superimposition of homodimeric ligand-free <i>Ma</i>Pgb*(III) (magenta) onto <i>Ma</i>...
Myoglobin is the subject of continuing investigations because of its ability to bind oxygen reversib...
<p>(A) Charmm_mini; (B) Charmm_ave; (C) Charmm_706ps. In the cartoon representations, the green and ...
<p>(a) Superposition of the YW/ELA/HLA-A2 and the DMF5/ELA/HLA-A2 complexes. DMF5 α chain is yellow,...
The structural factors governing azide and cyanide binding have been examined by measuring the effec...
<p>Residues lining the haem distal pocket are indicated and shown in stick representation (grey). Su...
<p>Residues lining the heme distal pocket are indicated (one letter code) and shown in green for the...
<p>Residues lining the haem distal pocket are indicated and shown in stick representation (yellow). ...
<p>Residues lining the haem distal pocket are indicated and shown in stick representation (brown). S...
<p>Residues lining the haem distal pocket are indicated and shown in stick representation (green) fo...
<p>(Panel A) The secondary structure elements are labeled A–H’. The 20 <i>N</i>-terminal residues an...
<p>A: Cartoon representation of the PttTrHb model in cyan colour. The heme is shown as sticks colour...
<p>Residues found in contact with F476 are depicted in sticks. Three distinct hydrophobic clusters a...
Bacillus megaterium flavocytochrorne P450 BM3 (CYP102A1) is a biotechnologically important cytochrom...
<p>Amino acid residues of L35P mutant through which hydrogen bonds exert influence from the site of ...
<p>(<b>A</b>) Superimposition of homodimeric ligand-free <i>Ma</i>Pgb*(III) (magenta) onto <i>Ma</i>...
Myoglobin is the subject of continuing investigations because of its ability to bind oxygen reversib...
<p>(A) Charmm_mini; (B) Charmm_ave; (C) Charmm_706ps. In the cartoon representations, the green and ...
<p>(a) Superposition of the YW/ELA/HLA-A2 and the DMF5/ELA/HLA-A2 complexes. DMF5 α chain is yellow,...
The structural factors governing azide and cyanide binding have been examined by measuring the effec...