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Protein Synthesis Animation Video - YouTube

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An interactive protein synthesis animation

Thus, hemoglobin's biological function is regulated by thechanging of the overall protein structure. This structure isaltered by the binding or releasing of CO2 and H+to the interfaces of the subunits in hemoglobin (Figure 8).

Protein Synthesis and the Lean, Mean Ribosome …

To understand the oxygen-binding properties of hemoglobin, wewill focus briefly on the structure of the protein and the metalcomplexes embedded in it.

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The shape change in the heme group has important implicationsfor the rest of the hemoglobin protein, as well. When the ironatom moves into the porphyrin plane upon oxygenation, thehistidine residue to which the iron atom is attached is drawncloser to the heme group. This movement of the histidine residuethen shifts the position of other amino acids that are near thehistidine (Figure 6). When the amino acids in a protein areshifted in this manner (by the oxygenation of one of the hemegroups in the protein), the structure of the interfaces betweenthe four subunits is altered. Hence, when a single heme group inthe hemoglobin protein becomes oxygenated, the whole proteinchanges its shape. In the new shape, it is easier for the otherthree heme groups to become oxygenated. Thus, the binding of onemolecule of O2 to hemoglobin enhances the ability ofhemoglobin to bind more O2 molecules. This property ofhemoglobin is known as "cooperative binding."

This is a molecular model of hemoglobin with the subunits displayed in the ribbon representation. A ribbon representation traces the backbone atoms of a protein and is often used to represent its three-dimensional structure. The four heme groups are displayed in the ball-and-stick representation.

Sickle Cell Anemia | HHMI BioInteractive

6: Nucleic Acids and Protein Synthesis




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