Effects of chemical exchange and dipole-dipole interactions on the proton relaxation rates of surface histidyl residues in human hemoglobins
Author:
Publisher
Elsevier BV
Subject
General Engineering
Reference33 articles.
1. Role of the .beta.146 histidyl residue in the alkaline Bohr effect of hemoglobin
2. A proton nuclear magnetic resonance investigation of histidyl residues in human normal adult hemoglobin
3. A proton nuclear magnetic resonance investigation of histidyl residues in sickle hemoglobin
4. Proton longitudinal relaxation investigation of histidyl residues in human normal adult hemoglobin
Cited by 3 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. Frequency Dependence of T1and T2Relaxation Times of Water in Normal and Tumoral Lung Tissues. T2Relaxation Time Evidence of Water Different Chemical Shifts and Exchange Rates.;Spectroscopy Letters;1994-06
2. pH-induced structural changes in human serum apotransferrin pKa values of histidine residues and N-terminal amino group determined by 1H-NMR spectroscopy;European Journal of Biochemistry;1994-03
3. Proton Nuclear Magnetic Resonance Studies On Hemoglobin: Cooperative Interactions And Partially Ligated Intermediates;Advances in Protein Chemistry Volume 43;1992
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