Search Results - "Murray, Lionel P"

Energy storage in the primary photochemical events of rhodopsin and isorhodopsin by Schick, G. Alan, Cooper, Thomas M, Holloway, Richard A, Murray, Lionel P, Birge, Robert R

“…The energetics associated with the photoequilibrium (Formula: see text) are measured at 77 K by using pulsed-laser photocalorimetry and a range of excitation…”
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Time-resolved optical spectroscopy and structural dynamics following photodissociation of carbonmonoxyhemoglobin by Murray, L P, Hofrichter, J, Henry, E R, Eaton, W A

“…A summary is presented of our current understanding of the kinetics of ligand rebinding and conformational changes at room temperature following…”
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Dynamics of the quaternary conformational change in trout hemoglobin by Hofrichter, James, Henry, Eric R, Szabo, Attila, Murray, Lionel P, Ansari, Anjum, Jones, Colleen M, Coletta, Massimo, Falcioni, Giancarlo, Brunori, Maurizio, Eaton, William A

“…The kinetics of conformational changes in trout hemoglobin I have been characterized over the temperature range 2-65 degrees C from time-resolved absorption…”
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Two-photon, carbon-13 and two-dimensional proton NMR spectroscopic studies of retinyl Schiff bases, protonated Schiff bases and Schiff base salts: evidence for a protonation induced .pi..pi. excited state level ordering reversal by Birge, Robert R, Murray, Lionel P, Zidovetzki, Raphael, Knapp, Henry M

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Two-Photon Spectroscopy of Locked-11-cis-rhodopsin: Evidence for a Protonated Schiff Base in a Neutral Protein Binding Site by Birge, Robert R., Murray, Lionel P., Pierce, Brian M., Akita, Hiroyukl, Balogh-Nair, Valeria, Findsen, Leonore A., Nakanishi, Koji

“…We studied the nature of the protein binding site of rhodopsin, using two-photon spectroscopy to assign the location of the low-lying ``covalent'' 1Ag* --like…”
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The Effect of Quaternary Structure on the Kinetics of Conformational Changes and Nanosecond Geminate Rebinding of Carbon Monoxide to Hemoglobin by Murray, Lionel P., Hofrichter, James, Henry, Eric R., Ikeda-Saito, Masao, Kitagishi, Keiko, Yonetani, Takashi, Eaton, William A.

“…To determine the effect of quaternary structure on the individual kinetic steps in the binding of carbon monoxide to the α subunit of hemoglobin, time-resolved…”
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