Molecular Stability of he Philly (α2β235 (C1) Tyr → Phe)
Author:
Publisher
Informa UK Limited
Subject
Biochemistry, medical,Clinical Biochemistry,Genetics(clinical),Hematology
Link
http://www.tandfonline.com/doi/pdf/10.3109/03630268108996923
Reference13 articles.
1. Structure and function of haemoglobin philly (Tyr C1 (35) β→Phe)
2. Hemoglobin Philly (β35 tyrosine→phenylalanine): studies in the molecular pathology of hemoglobin
3. Denatured hemoglobin in sickle erythrocytes.
4. A New Method for the Preparation of α and β Subunits of Human Hemoglobin
5. Properties of the α and β Chains of Hemoglobin Prepared from Their Mercuribenzoate Derivatives by Treatment with 1-Dodecanethiol
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2. Characterization of a 12 kDa Thermal-Stable Antigenic Protein in Bovine Blood;Journal of Food Science;2011-10-04
3. Site-directed mutations of human hemoglobin at residue 35β: A residue at the intersection of the α1β1, α1β2, and α1α2 interfaces;Protein Science;2001-09
4. Effects of β6 amino acid hydrophobicity on stability and solubility of hemoglobin tetramers;FEBS Letters;1993-01-02
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