Erstellt von Charlotte Hewson
vor mehr als 9 Jahre
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Frage | Antworten |
what is the primary structure of haemoglobin? | four polypeptide chains |
what is the secondary structure of haemoglobin? | each polypeptide chain is wound into a helix |
what is the tertiary structure of haemoglobin? | each polypeptide chain is folded into a precise shape - an important factor in its ability to carry oxygen |
what is the quaternary structure of haemoglobin? | -all four polypeptides are linked together to form an almost spherical molecule. -each polypeptide is associated with a haem group. |
what ion is contained within the haem group? | ferrous ion (Fe2+) |
how many molecules can be combined to one haemoglobin molecule? | 4 |
how many oxygen atoms can be combined on one haemoglobin? | 8 (because each oxygen molecule has 2 oxygen atoms) |
what is haemoglobins main role? | to transport oxygen |
how is haemoglobin efficient at transporting oxygen? | -readily associate with oxygen at the surface where gas exchange takes place -readily dissociate from oxygen at the tissues that need it. |
why are there different types of haemoglobin? | high affinity - take oxygen easily and release less readily low affinity - take up less easily and release readily |
what type of haemoglobin would an organism living in an environment with little oxygen need? | high affinity |
what type of haemoglobin would an organism with high metabolic rate need? | low affinity provided there is sufficient oxygen in the air. |
what is the process called where haemoglobin combines with oxygen? | loading or associating |
where does loading/associating happen in humans? | the lungs |
what is the name of the process in which haemoglobin releases the oxygen? | unloading or dissociating |
where does dissociation/unloading occur in humans? | in the tissues |
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