Role of hydrophobicity of phenylalanine beta 85 and leucine beta 88 in the acceptor pocket for valine beta 6 during hemoglobin S polymerization.
Open Access
- 1 December 1994
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 269 (50) , 31563-31566
- https://doi.org/10.1016/s0021-9258(18)31730-7
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Effects of β6 amino acid hydrophobicity on stability and solubility of hemoglobin tetramersFEBS Letters, 1993
- HB Shelby [β131(H9)GLN→LYS] in Association with HB S [β6(A3)GLU→VAL]: Characterization, Stability, and Effects on HB S PolymerizationHemoglobin, 1993
- Effect of amino acid at the beta 6 position on surface hydrophobicity, stability, solubility, and the kinetics of polymerization of hemoglobin. Comparisons among Hb A (Glu beta 6), Hb C (Lys beta 6), Hb Machida (Gln beta 6), and Hb S (Val beta 6).Journal of Biological Chemistry, 1987
- Interaction of Hemoglobin Siriraj with Hemoglobin S: A Mild Sickle Cell SyndromeHemoglobin, 1986
- Mechanical precipitation of hemoglobin KölnBiochimica et Biophysica Acta (BBA) - Protein Structure, 1975
- Crystal structure of sickle-cell deoxyhemoglobin at 5 Å resolutionJournal of Molecular Biology, 1975
- Abnormal Precipitation of Oxyhemoglobin S by Mechanical ShakingProceedings of the National Academy of Sciences, 1974
- A New Unstable Haemoglobin: Hb Buenos Aires, β85 (F1) Phe→SerActa Haematologica, 1973
- New Unstable Haemoglobin Borås: β88 (F4) Leucine→ArginineNature, 1969
- Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution: The Atomic ModelNature, 1968