Mutational destabilization of the critical interface water cluster in Scapharca dimeric hemoglobin: structural basis for altered allosteric activity (original ) (raw )Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobin
William Royer
Proceedings of the National Academy of Sciences, 1996
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Cooperativity in Scapharca dimeric hemoglobin: simulation of binding intermediates and elucidation of the role of interfacial water
Yaoqi Zhou
Journal of molecular biology, 2003
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Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7-A resolution
Peter Condon
Journal of Biological Chemistry, 1994
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Crystal Structure of Oxygenated Scapharca Dimeric Hemoglobin at 1.7 Angstroms Resolution
Peter Condon
1994
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The Mutation K30D Disrupts the Only Salt Bridge at the Subunit Interface of the Homodimeric Hemoglobin from Scapharca inaequivalvis and Changes the Mechanism of Cooperativity
Pierpaolo Ceci
Journal of Biological Chemistry, 2002
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A Single Mutation (Thr72→Ile) at the Subunit Interface is Crucial for the Functional Properties of the Homodimeric Co-operative Haemoglobin fromScapharca inaequivalvis
Francesca Polizio
Journal of Molecular Biology, 1995
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Restricting the Ligand-Linked Heme Movement in Scapharca Dimeric Hemoglobin Reveals Tight Coupling between Distal and Proximal Contributions to Cooperativity †
William Royer
Biochemistry, 2001
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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
Giovanni Ciccotti
Biophysical Journal, 1998
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Mutation of Residue Phe97 to Leu Disrupts the Central Allosteric Pathway in Scapharca Dimeric Hemoglobin
William Royer
Journal of Biological Chemistry, 1997
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Cooperative oxygen binding to Scapharca inaequivalvis hemoglobin in the crystal
stefano bettati
Journal of Biological …, 1996
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The homodimeric hemoglobin from Scapharca can be locked into new cooperative structures upon reaction of Cys92, located at the subunit interface, with organomercurials
Emilia Chiancone
FEBS Letters, 1992
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Tertiary and Quaternary Allostery in Tetrameric Hemoglobin from Scapharca inaequivalvis
Stefano Bettati
Biochemistry, 2013
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Effects of mutations on the molecular dynamics of oxygen escape from the dimeric hemoglobin of Scapharca inaequivalvis
Kevin Trujillo
F1000Research, 2015
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Role of subunit interfaces in the allosteric mechanism of hemoglobin
Joel Janin
Proceedings of the National Academy of Sciences, 1976
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Residue F4 Plays a Key Role in Modulating Oxygen Affinity and Cooperativity in Scapharca Dimeric Hemoglobin †
William Royer
Biochemistry, 2005
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Structural and functional effects of selective chemical modifications of Scapharca inaequivalvis haemoglobins in relation to their unique assembly
A. Boffi
Biochemical Journal, 1987
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Ligand and interfacial dynamics in a homodimeric hemoglobin
Prashant Gupta
Structural Dynamics, 2016
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Stereodynamic properties of the cooperative homodimeric Scapharca inaequivalvis hemoglobin studied through optical absorption spectroscopy and ligand rebinding kinetics
Emilia Chiancone , Antonio Cupane , A. Boffi
Biophysical Journal, 1994
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Functional consequences of mutations at the allosteric interface in hetero‐ and homo‐hemoglobin tetramers
O. Schaad
Protein Science, 1993
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Nuclear-magnetic-resonance investigation of the cooperative homodimeric hemoglobin from the mollusc Scapharca inaequivalvis. Molecular and electronic structure of the cyano-met derivative
Emilia Chiancone
European Journal of Biochemistry, 1989
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Ligand Uptake Modulation by Internal Water Molecules and Hydrophobic Cavities in Hemoglobins
Diego Gauto
The Journal of Physical Chemistry B, 2014
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X-Ray crystallographic structural characteristics of Arabidopsis hemoglobin I and their functional implications
jagreet kaur
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013
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Hydroxide Rather Than Histidine Is Coordinated to the Heme in Five-coordinate Ferric Scapharca inaequivalvis Hemoglobin
A. Boffi
Journal of Biological Chemistry, 1999
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Interfacial and Distal-Heme Pocket Mutations Exhibit Additive Effects on the Structure and Function of Hemoglobin †
Virgil Simplaceanu
Biochemistry, 2008
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Allosteric mechanism of haemoglobin: rupture of salt-bridges raises the oxygen affinity of the T-structure
stefano bettati
Journal of Molecular Biology, 1998
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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
Emilia Chiancone
Archives of Biochemistry and Biophysics, 1997
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Crystalline Ligand Transitions in Lamprey Hemoglobin. STRUCTURAL EVIDENCE FOR THE REGULATION OF OXYGEN AFFINITY
William Royer
Journal of Biological Chemistry, 2001
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The 2.0 Å Crystal Structure ofScapharcaTetrameric Hemoglobin: Cooperative Dimers within an Allosteric Tetramer
Emilia Chiancone
Journal of Molecular Biology, 1995
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Crystallographic Evidence for a New Ensemble of Ligand-Induced Allosteric Transitions in Hemoglobin: The T-to-THigh Quaternary Transitions
Jeffrey Kavanaugh
Biochemistry, 2005
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Tertiary and quaternary effects in the allosteric regulation of animal hemoglobins
Luca Ronda
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013
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H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin
JUAN AARON GAMARRA BUSTAMANTE
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013
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