Conformational Changes in Hemoglobin S (βE6V) Imposed by Mutation of the βGlu7–βLys132 Salt Bridge and Detected by UV Resonance Raman Spectroscopy-Reference-Cited by-同舟云学术

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Conformational Changes in Hemoglobin S (βE6V) Imposed by Mutation of the βGlu7–βLys132 Salt Bridge and Detected by UV Resonance Raman Spectroscopy

Published:2003-02 Issue:9 Volume:278 Page:7257-7263
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Juszczak Laura J.,Fablet Christophe,Baudin-Creuza Veronique,Lesecq-Le Gall Sophie,Hirsch Rhoda Elison,Nagel Ronald L.,Friedman Joel M.,Pagnier Josée

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference35 articles.

1. Functional Studies and Polymerization of Recombinant Hemoglobin Glu-α2β26(A3) → Val/Glu-7(A4) → Ala

2. Influence of the A Helix Structure on the Polymerization of Hemoglobin S

3. [22] Resonance raman spectroscopy of hemoglobin

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1. Photolyses of mammalian carboxy-hemoglobin studied by photoacoustic calorimetry;Science China Physics, Mechanics and Astronomy;2013-05-23

2. Raman Spectroscopy Study of the Effect of H+ on the Oxygen Affinity Capacity of Hemoglobin;SPECTROSC SPECT ANAL;2013

3. Genetically Engineered Polypeptides as a Model of Intrinsically Disordered Fibrillogenic Proteins: Deep UV Resonance Raman Spectroscopic Study;Instrumental Analysis of Intrinsically Disordered Proteins;2010-09-09

4. Advanced Statistical and Numerical Methods for Spectroscopic Characterization of Protein Structural Evolution;Chemical Reviews;2010-07-02

5. Phase Separation and Crystallization of Hemoglobin C in Transgenic Mouse and Human Erythrocytes;Biophysical Journal;2008-10

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