BioChem Chapter 10
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Created by:
KathyDiane on November 2, 2011
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Hemoglobin
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30 terms
Terms | Definitions |
|---|---|
 Heterotetramer | A protein containing four non-covalently bound subunits where in the subunits are not all identical. |
| Homotetramer | A protein consisting of four identical subunits |
| Hemoglobin | - 65 KD -two alpha subunits -Heterotetramer Transports oxygen from lungs to tissue -Heme protetic group - Hb |
| Substrate | Molecules that enzymes act upon |
| Ligand | A substance that forms a complex with a molecule to serve a biological purpose (single Triggering Molecule) |
| Active Site | Location where the ligand or substrate binds |
| Prosthetic group | Compound permanently associated with a protein that contributes to the proteins function |
| Co-factor | a prosthetic group that is bound to enzymes |
| Subunit | A single protein molecule that assembles with another protein to form a protein complex |
| Porphyrin | a basic structure of the blood carrying pigment (hemoglobin) in red blood cells (Contains a metal) |
| Protoporphyrin | Porphrin without a metal |
| Fe 2+ | Ferrous Binds oxygen |
| Fe 3+ | Ferric does not bind oxygen |
| Myoglobin | -Mb -Transports oxygen in muscle tissue and also stores it - one subunit = 153 AA - 78% of amino acids are in alpha helices - His 93 Binds to heme |
| Beta chain in hemoglobin | 146 amino acids (Lack D Helix) |
| Alpha chain in hemoglobin | 141 Amino acids |
| Cooperative Binding | as more molecules of oxygen are added the bond strength between them increases |
| Allosteric protein | a protein whose shape is changed when it binds to a particular molecule. In the new shape the proteins ability to react to a second molecule is altered |
| Hill equation | gives a number for the binding sites of a protein |
| Hill Plot | Graph of the hill equation |
| Hill coefficient | Determines if the ligand will bind or not |
| Hill Coefficient = 1 | Not cooperatively binding |
| Hill coefficient = greater than 1 | Positive cooperative binding |
| Hill Coefficient = less than 1 | Negative cooperative binding |
| MWC model | All subunits undergo transition at the same time |
| Sequential (induced fit) model | Individual subunits can be in different conformations |
| H+ binding to Hb | Binds to his 146 makes an ion pair which created a salt bridge that helps stabilize the t-state |
| CO2 binding to Hb | Binds to the n-terminal amino group the charge created makes a salt bridge |
| Binding of BPG to Hb | Lowers the affinity for oxygen binding and makes it easier to release oxygen from Hb |
| Single point mutation creating sickle cell anemia | The mutation caused long chains of Hb to be made creating the sickle shape |
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