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  2. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    Hemoglobin has an oxygen-binding capacity of 1.34 mL of O 2 per gram, [6] which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood plasma alone. [7] The mammalian hemoglobin molecule can bind and transport up to four oxygen molecules. [8] Hemoglobin also transports other gases.

  3. Hemoglobin A - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin_A

    Hemoglobin A (HbA), also known as adult hemoglobin, hemoglobin A1 or α 2 β 2, is the most common human hemoglobin tetramer, accounting for over 97% of the total red blood cell hemoglobin. [1] Hemoglobin is an oxygen-binding protein, found in erythrocytes , which transports oxygen from the lungs to the tissues. [ 2 ]

  4. Globin - Wikipedia

    en.wikipedia.org/wiki/Globin

    The most famous mutation in the globin fold is a change from glutamate to valine in one chain of the hemoglobin molecule. This mutation creates a "hydrophobic patch" on the protein surface that promotes intermolecular aggregation, the molecular event that gives rise to sickle-cell disease. [citation needed]

  5. Oxygen–hemoglobin dissociation curve - Wikipedia

    en.wikipedia.org/wiki/Oxygenhemoglobin...

    Each hemoglobin molecule has the capacity to carry four oxygen molecules. These molecules of oxygen bind to the globin chain of the heme prosthetic group. [1] When hemoglobin has no bound oxygen, nor bound carbon dioxide, it has the unbound conformation (shape). The binding of the first oxygen molecule induces change in the shape of the ...

  6. Heme - Wikipedia

    en.wikipedia.org/wiki/Heme

    For example, the ability of hemoglobin to effectively deliver oxygen to tissues is due to specific amino acid residues located near the heme molecule. [13] Hemoglobin reversibly binds to oxygen in the lungs when the pH is high, and the carbon dioxide concentration is low. When the situation is reversed (low pH and high carbon dioxide ...

  7. Cooperativity - Wikipedia

    en.wikipedia.org/wiki/Cooperativity

    One oxygen molecule can bind to the ferrous iron of a heme molecule in each of the four chains of a hemoglobin molecule. Deoxy-hemoglobin has a relatively low affinity for oxygen, but when one molecule binds to a single heme, the oxygen affinity increases, allowing the second molecule to bind more easily, and the third and fourth even more easily.

  8. Today's Wordle Hint, Answer for #1252 on Friday, November 22 ...

    www.aol.com/lifestyle/todays-wordle-hint-answer...

    Today's Wordle Answer for #1252 on Friday, November 22, 2024. Today's Wordle answer on Friday, November 22, 2024, is PEARL. How'd you do? Next: Catch up on other Wordle answers from this week.

  9. Iron in biology - Wikipedia

    en.wikipedia.org/wiki/Iron_in_biology

    In hemoglobin, the iron is in one of four heme groups and has six possible coordination sites; four are occupied by nitrogen atoms in a porphyrin ring, the fifth by an imidazole nitrogen in a histidine residue of one of the protein chains attached to the heme group, and the sixth is reserved for the oxygen molecule it can reversibly bind to. [5]