Protein Conformational Dynamics of Homodimeric Hemoglobin Revealed by Combined Time-Resolved Spectroscopic Probes

Protein Conformational Dynamics of Homodimeric Hemoglobin Revealed by Combined Time-Resolved Spectroscopic Probes

Allosteric regulation: The protein kinetics of the R–T transition of homodimeric hemoglobin (HbI) in solution are investigated using combined spectroscopic probes (see figure). The comparative results using both transient absorption spectroscopy and transient grating techniques show that the former...

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Veröffentlicht in:Chemphyschem 2010-01, Vol.11 (1), p.109-114
Hauptverfasser: Choi, Jungkweon, Muniyappan, Srinivasan, Wallis, John T., Royer Jr, William E., Ihee, Hyotcherl
Format: Artikel
Sprache:eng
Schlagworte:
Animals
Biological and medical sciences
Calorimetry
Conformational dynamics in molecular biology
Fundamental and applied biological sciences. Psychology
Hemoglobins - chemistry
homodimeric hemoglobin
Lasers
Molecular biophysics
Molecular Dynamics Simulation
Protein Conformation
Protein Multimerization
protein structures
Scapharca - chemistry
Spectrum Analysis
structure-activity relationships
Thermodynamics
time-resolved spectroscopy
transient grating
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Zusammenfassung:Allosteric regulation: The protein kinetics of the R–T transition of homodimeric hemoglobin (HbI) in solution are investigated using combined spectroscopic probes (see figure). The comparative results using both transient absorption spectroscopy and transient grating techniques show that the former can be blind to the overall quaternary structural change.
ISSN:1439-4235
1439-7641
DOI:10.1002/cphc.200900822