Relaxation amplitude analysis of thiocyanate and formate binding to human aquomethemoglobin A-Reference-Cited by-同舟云学术

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Relaxation amplitude analysis of thiocyanate and formate binding to human aquomethemoglobin A

Published:1985-07 Issue:3 Volume:829 Page:327-334
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Iheanyichukwu Iwuoha E.,Kehinde Onwochei Okonjo

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference23 articles.

1. High resolution nuclear magnetic resonance spectra of hemoglobin

2. Ligand binding and internal equilibiums in proteins

3. Relation between structure, co-operativity and spectra in a model of hemoglobin action

4. Conformation and spin state in methemoglobin.

5. Interaction of methemoglobin with inositol hexaphosphate. Presence of the T state in human adult methemoglobin in the low spin state.

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Static and dynamic effects in spin equilibrium systems;Coordination Chemistry Reviews;1988-05

2. Subunit iron spin heterogeneity in human aquomethemoglobin A;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1986-09

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