Hemoglobin: Difference between revisions
Eran Hodis (talk | contribs) |
Eran Hodis (talk | contribs) |
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This view of the <scene name='Hemoglobin/Hydrophob1/2'>beta chain</scene> shows charged amino acids (lime green), polar amino acids (dark green), hydrophobic amino acids (grey), heme (tan), and water oxygens (light blue). Charged and polar amino acids are common on the surface, where they form hydrogen bonds with water. Most water is not shown. Protein structures tend to fold in such a way so that their hydrophobic residues are buried and their hydrophilic residues are on the surface. A vertical slice through the molecule near the front surface, shows <scene name='Hemoglobin/Hydrophob2/1'>many hydrophilic residues</scene>. As we move the slice plane <scene name='Hemoglobin/Hydrophob3/1'>deeper</scene> into the molecule, the center is hydrophobic while the surfaces have many polar and charged residues. We can move the slab <scene name='Hemoglobin/Hydrophob5/1'>deeper</scene>, and <scene name='Hemoglobin/Hydrophob6/1'>deeper still</scene>. Near the rear surface, hydrophilic residues are <scene name='Hemoglobin/Hydrophob7/1'>again common</scene>. | This view of the <scene name='Hemoglobin/Hydrophob1/2'>beta chain</scene> shows charged amino acids (lime green), polar amino acids (dark green), hydrophobic amino acids (grey), heme (tan), and water oxygens (light blue). Charged and polar amino acids are common on the surface, where they form hydrogen bonds with water. Most water is not shown. Protein structures tend to fold in such a way so that their hydrophobic residues are buried and their hydrophilic residues are on the surface. A vertical slice through the molecule near the front surface, shows <scene name='Hemoglobin/Hydrophob2/1'>many hydrophilic residues</scene>. As we move the slice plane <scene name='Hemoglobin/Hydrophob3/1'>deeper</scene> into the molecule, the center is hydrophobic while the surfaces have many polar and charged residues. We can move the slab <scene name='Hemoglobin/Hydrophob5/1'>deeper</scene>, and <scene name='Hemoglobin/Hydrophob6/1'>deeper still</scene>. Near the rear surface, hydrophilic residues are <scene name='Hemoglobin/Hydrophob7/1'>again common</scene>. | ||
==Section== | ==Section Under Construction== | ||
Contents of file HbAllo.kin: | Contents of file HbAllo.kin: | ||
*{Kin 1}* An exercise in allostery - a hemoglobin subunit binding O2 | *{Kin 1}* An exercise in allostery - a hemoglobin subunit binding O2 | ||