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  • 1
    Publication Date: 1992-06-26
    Description: Nanosecond lasers were used to measure the rate of conformational changes in myoglobin after ligand dissociation at ambient temperatures. At low solvent viscosities the rate is independent of viscosity, but at high viscosities it depends on approximately the inverse first power of the viscosity. Kramers theory for unimolecular rate processes can be used to explain this result if the friction term is modified to include protein as well as solvent friction. The theory and experiment suggest that the dominant factor in markedly reducing the rate of conformational changes in myoglobin at low temperatures (less than 200 K) is the very high viscosity (greater than 10(7) centipoise) of the glycerol-water solvent. That is, at low temperatures conformational substates may not be "frozen" so much as "stuck."〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ansari, A -- Jones, C M -- Henry, E R -- Hofrichter, J -- Eaton, W A -- New York, N.Y. -- Science. 1992 Jun 26;256(5065):1796-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1615323" target="_blank"〉PubMed〈/a〉
    Keywords: Carbon Monoxide ; Hot Temperature ; Lasers ; Myoglobin/*chemistry ; Protein Conformation ; Solvents/*adverse effects ; Spectrophotometry, Atomic ; Viscosity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1987-07-31
    Description: A laser photolysis technique has been developed to assess the quantitative significance of the delay time of hemoglobin S gelation to the pathophysiology of sickle cell disease. Changes in the saturation of hemoglobin S with carbon monoxide produced by varying the intensity of a photolytic laser beam were used to simulate changes in the saturation of oxyhemoglobin S produced by variations in oxygen pressure. The presence of polymer at steady-state saturation with carbon monoxide was determined by measurement of the kinetics of gelation after complete photodissociation. The kinetics are a very sensitive probe for polymer since small amounts of polymerized hemoglobin increase the rate of nucleation sufficiently to eliminate the delay period. First, the equilibrium gelation properties of partially photodissociated carbonmonoxyhemoglobin S were shown to be the same as partially oxygenated hemoglobin S, and the method was then used to determine the effect of saturation on the formation and disappearance of polymers in individual sickle cells. The saturation at which polymers first formed upon deoxygenation was much lower than the saturation at which polymers disappeared upon reoxygenation. The results indicate that at venous saturations with oxygen, gelation takes place in most cells at equilibrium, but is prevented from occurring in vivo because the delay times are sufficiently long that most cells return to the lungs and are reoxygenated before polymerization has begun.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mozzarelli, A -- Hofrichter, J -- Eaton, W A -- New York, N.Y. -- Science. 1987 Jul 31;237(4814):500-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3603036" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/*blood ; Biopolymers ; Carbon Monoxide/blood ; Erythrocytes, Abnormal/*metabolism ; Gels ; Hemoglobin, Sickle/*metabolism ; Humans ; Kinetics ; Lasers ; Light ; Oxygen/blood ; Photolysis ; Scattering, Radiation ; Spectrophotometry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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