Mutational destabilization of the critical interface water cluster in Scapharca dimeric hemoglobin: structural basis for altered allosteric activity (original) (raw)

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Restricting the Ligand-Linked Heme Movement in Scapharca Dimeric Hemoglobin Reveals Tight Coupling between Distal and Proximal Contributions to Cooperativity †

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Structural and Dynamic Properties of the Homodimeric Hemoglobin from Scapharca inaequivalvis Thr-72→Ile Mutant: Molecular Dynamics Simulation, Low Temperature Visible Absorption Spectroscopy, and Resonance Raman Spectroscopy Studies

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Residue F4 Plays a Key Role in Modulating Oxygen Affinity and Cooperativity in Scapharca Dimeric Hemoglobin †

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Structural and functional effects of selective chemical modifications of Scapharca inaequivalvis haemoglobins in relation to their unique assembly

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Hydroxide Rather Than Histidine Is Coordinated to the Heme in Five-coordinate Ferric Scapharca inaequivalvis Hemoglobin

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Interfacial and Distal-Heme Pocket Mutations Exhibit Additive Effects on the Structure and Function of Hemoglobin †

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The Unique Heme–Heme Interactions of the HomodimericScapharca inaequivalvisHemoglobin as Probed in the Protein Reconstituted with Unnatural 2,4 Heme Derivatives

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H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin

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