L
L. Eisenstein
Researcher at University of Illinois at Urbana–Champaign
Publications - 37
Citations - 3705
L. Eisenstein is an academic researcher from University of Illinois at Urbana–Champaign. The author has contributed to research in topics: Bacteriorhodopsin & Myoglobin. The author has an hindex of 22, co-authored 37 publications receiving 3634 citations.
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Journal ArticleDOI
Dynamics of ligand binding to myoglobin
TL;DR: The nonexponential rebinding observed at low temperatures and in solid samples implies that the innermost barrier has a spectrum of activation energies, similar to how myoglobin achieves specificity and order.
Journal ArticleDOI
Solvent viscosity and protein dynamics
D. Beece,L. Eisenstein,Hans Frauenfelder,D. Good,M. C. Marden,Lou Reinisch,A. H. Reynolds,Larry B. Sorensen,Kwok To Yue +8 more
TL;DR: In this article, the binding of CO to protoheme and O2 and CO to myoglobin in many different solvents was studied, and the transition rates in heme-CO are inversely proportional to the solvent viscosity and can consequently be described by the Kramers equation.
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Control and pH dependence of ligand binding to heme proteins
W Doster,D. Beece,S. F. Bowne,Ernesto E. DiIorio,L. Eisenstein,Hans Frauenfelder,Lou Reinisch,E. Shyamsunder,K. H. Winterhalter,Kwok To Yue +9 more
TL;DR: In this article, the recombination after flash photolysis of dioxygen and carbon monoxide with sperm whale myoglobin (Mb), and separated beta chains of human hemoglobin (beta A) and hemoglobin Zurich (beta ZH), has been studied as a function of pH and temperature from 300 to 60 K.
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Fourier transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts.
TL;DR: In this paper, Fourier transform infrared difference spectroscopy has been used to obtain the vibrational modes in the chromophore and apoprotein that change in intensity or position between light-adapted bacteriorhodopsin and the K and M intermediates in its photocycle.
Journal ArticleDOI
Infrared spectroscopy of photodissociated carboxymyoglobin at low temperatures
J. O. Alben,D. Beece,S F Bowne,W Doster,L. Eisenstein,Hans Frauenfelder,D. Good,J D McDonald,M. C. Marden,P. P. Moh,Lou Reinisch,A. H. Reynolds,E. Shyamsunder,K T Yue +13 more
TL;DR: The observation of essentially free CO in state B implies that the difference between Mb and deoxyMb is not due to an interaction of the flashed-off ligand with the protein but is caused by an incomplete relaxation of the protein structure at low temperatures.