Alteration of Axial Coordination by Protein Engineering in Myoglobin - Wikidata - thesis-toulmin - TriplyDB

Alteration of Axial Coordination by Protein Engineering in Myoglobin

Alteration of Axial Coordination by Protein Engineering in Myoglobin

http://www.wikidata.org/entity/Q57610393

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Biophysical and structural analysis of a novel heme B iron ligation in the flavocytochrome cellobiose dehydrogenase The crystal structure of Synechocystis hemoglobin with a covalent heme linkage A cis-Proline in -Hemoglobin Stabilizing Protein Directs the Structural Reorganization of -Hemoglobin Rational design of heterodimeric protein using domain swapping for myoglobin A novel tyrosine-heme C−O covalent linkage in F43Y myoglobin: a new post-translational modification of heme proteins How a novel tyrosine-heme cross-link fine-tunes the structure and functions of heme proteins: a direct comparitive study of L29H/F43Y myoglobin Distinct roles of a tyrosine-associated hydrogen-bond network in fine-tuning the structure and function of heme proteins: two cases designed for myoglobin Human myoglobin recognition of oxygen: dynamics of the energy landscape.Regulation of aldoxime dehydratase activity by redox-dependent change in the coordination structure of the aldoxime-heme complex.Regulating the coordination state of a heme protein by a designed distal hydrogen-bonding network.The effects of heme pocket hydrophobicity on the ligand binding dynamics in myoglobin as studied with leucine 29 mutants.Evidence that the heme regulatory motifs in heme oxygenase-2 serve as a thiol/disulfide redox switch regulating heme binding Investigation of the haem-nicotinate interaction in leghaemoglobin. Role of hydrogen bonding.A structural model for the membrane-integral domain of succinate: quinone oxidoreductases.Protein engineering strategies for designing more stable hemoglobin-based blood substitutes.Oxygen affinity and amino acid sequence of myoglobins from endothermic and ectothermic fish.Haemophore-mediated bacterial haem transport: evidence for a common or overlapping site for haem-free and haem-loaded haemophore on its specific outer membrane receptor.Residues in the distal heme pocket of neuroglobin. Implications for the multiple ligand binding steps.Modifications of hemoglobin and myoglobin by Maillard reaction products (MRPs).

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Alteration of Axial Coordination by Protein Engineering in Myoglobin

http://www.wikidata.org/entity/Q57610393

description

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

im Juli 1995 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published in Journal of Biological Chemistry

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в липні 1995

@uk

name

Alteration of Axial Coordination by Protein Engineering in Myoglobin

@en

Alteration of Axial Coordination by Protein Engineering in Myoglobin

@nl

type

label

Alteration of Axial Coordination by Protein Engineering in Myoglobin

@en

Alteration of Axial Coordination by Protein Engineering in Myoglobin

@nl

prefLabel

Alteration of Axial Coordination by Protein Engineering in Myoglobin

@en

Alteration of Axial Coordination by Protein Engineering in Myoglobin

@nl

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JBC.270.27.15993

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Journal of Biological Chemistry

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Alteration of Axial Coordination by Protein Engineering in Myoglobin

@en

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Anthony J. Wilkinson

http://www.w3.org/2001/XMLSchema#string

Graham N. George

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Ingrid J. Pickering

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John S. Olson

http://www.w3.org/2001/XMLSchema#string

Masao Ikeda-Saito

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Roger C. Prince

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Suzanne J. Admiraal

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Szymon Krzywda

http://www.w3.org/2001/XMLSchema#string

Tiansheng Li

http://www.w3.org/2001/XMLSchema#string

Yi Dou

http://www.w3.org/2001/XMLSchema#string

P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Distal pocket polarity in ligand binding to myoglobin: structural and functional characterization of a threonine68(E11) mutant

X-ray crystal structure of the ferric sperm whale myoglobin: imidazole complex at 2.0 A resolution

Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin

Structural and functional effects of apolar mutations of the distal valine in myoglobin

High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin

Distal pocket polarity in ligand binding to myoglobin: deoxy and carbonmonoxy forms of a threonine68(E11) mutant investigated by X-ray crystallography and infrared spectroscopy

Structural determinants of the stretching frequency of CO bound to myoglobin

Ab initio curved-wave x-ray-absorption fine structure.

Perturbations of the distal heme pocket in human myoglobin mutants probed by infrared spectroscopy of bound CO: correlation with ligand binding kinetics

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15993-16001

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scholarly article

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10.1074/JBC.270.27.15993

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27

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270

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1995-07-07T00:00:00Z

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