Structural and functional studies of Hb rothschild β 37 (C3) TRP → ARG A new variant of the α1β2contact
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(77)80593-0/fullpdf
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1. Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution: The Atomic Model
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4. HAEMOGLOBINS WITH ALTERED OXYGEN AFFINITY
5. Hemoglobin Hirose: α2β237(C3) Tryptophan Yielding Serine
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1. Hemoglobin Rothschild: Structural Rationalization of Decreased O2Affinity as a Consequence of a β37(C3)Trp→Arg Mutation;2024-06-06
2. Hb Alessandria [β37(C3)Trp→Leu; HBB: c.113G>T]: a Novel Variant on the β-Globin Chain with Slightly Increased Affinity for Oxygen Detected by Capillary Electrophoresis;Hemoglobin;2022-07-04
3. Role of hemoglobin structural-functional relationships in oxygen transport;Molecular Aspects of Medicine;2022-04
4. Hemoglobinopathies;Japanese Journal of Transfusion and Cell Therapy;2022-02-25
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