| Term 
 | Definition 
 
        | Carbonyl group forms a salt bridge with Lys40 (α-chain). Communication between α and B chains |  | 
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        | Term 
 | Definition 
 
        | Small AA, needed for close association of B/E helices |  | 
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        | Term 
 | Definition 
 
        | Forms a salt link with the imidazole group of His146 |  | 
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        | Term 
 | Definition 
 
        | H-bonds with carbonyl of Val98 |  | 
        |  | 
        
        | Term 
 | Definition 
 
        | Carbonyl of Val98 H-bond with Tyr 145 hydroxyl |  | 
        |  | 
        
        | Term 
 | Definition 
 
        | Distal Histidine. Forces "bent" binding of CO (reduced affinity). |  | 
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        | Term 
 | Definition 
 
        | Proximal Histidine. Coordinated to Fe of heme |  | 
        |  | 
        
        | Term 
 
        | Where does 2,3-bisphosphoglycerate bind? |  | Definition 
 
        | In space between the 4 globin subunits. 1 2,3-BPG per hemoglobin molecule. Stabilizes the T-form |  | 
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        | Term 
 
        | How does cooperativity work? |  | Definition 
 
        | 1. O2 binds, pulling Fe into plane of heme. 2. This moves the F-helix (via His92) 3. H-bond between Val98 carbonyl and Tyr145 hydroxyl is broken 4. Disruption of ionic interaction between His146 imidazole and Asp94 carboxylate 5. Disruption of His146 carbonyl and Lys40 amino group (α-chain) |  | 
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        | Term 
 
        | What is the importance of the Lys side chains in the heme pocket? |  | Definition 
 
        | Ensure correct positioning of the Heme group in the pocket |  | 
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