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Heme groups crevasse

S.3.2.4 The Disposition of Charged Side Chains Associated with the Crevasse Connecting the P - and a -Heme Groups for deoxyHb... [Pg.271]

There are basically two ways in which charged side chains of amino acid residues can lower their free energy when confronted with a hydrophobic domain. One way is to form ion pairs. TTie second way, when possible, is to move toward locations more remote from the most hydrophobic surface. Both examples are shown in the crevasse that connects the p and heme groups as well as in the equivalent crevasse connecting the a P -heme groups. [Pg.271]

From the perspective of the consilient mechanism, the approach of an oxygen molecule to a heme of deoxyhemoglobin faces loss of hydration as it enters the sphere of hydrophobic hydration emanating from the hydrophobic heme group and its hydrophobic surroundings, including that of the interheme crevasse. This constitutes AG,p and kinetic barriers. [Pg.278]

Figure 7.20. (A) Human deoxyhemoglobin Same stereo view as in Figure 7.19 of the pW interface axis looking directly into the inter-heme crevasse with an oc -chain on the right and a P -chain on the left, and shadings of groups as indicated in Figure 7.19, but in this case using the stick representation. Key residues are labeled. (B) Same as in A but the water mole-... Figure 7.20. (A) Human deoxyhemoglobin Same stereo view as in Figure 7.19 of the pW interface axis looking directly into the inter-heme crevasse with an oc -chain on the right and a P -chain on the left, and shadings of groups as indicated in Figure 7.19, but in this case using the stick representation. Key residues are labeled. (B) Same as in A but the water mole-...

See other pages where Heme groups crevasse is mentioned: [Pg.271]    [Pg.264]    [Pg.265]    [Pg.265]    [Pg.270]    [Pg.271]    [Pg.272]    [Pg.274]    [Pg.275]   


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