Search Results - "Eftink, M R"

The use of fluorescence methods to monitor unfolding transitions in proteins by Eftink, M.R.

“…This article discusses several strategies for the use steady-state and time-resolved fluorescence methods to monitor unfolding transitions in proteins. The…”
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Fluorescence techniques for studying protein structure by Eftink, M R

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The use of fluorescence methods to monitor unfolding transitions in proteins by Eftink, M R

“…The advantages and some limitations of the use of fluorescence methods for the quantitative determination of the thermodynamics of protein unfolding…”
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Biosynthetic incorporation of tryptophan analogues into staphylococcal nuclease: Effect of 5‐hydroxytryptophan and 7‐azatryptophan on structure and stability by Wong, Cing‐Yuen, Eftink, Maurice R.

“…5‐Hydroxytryptophan (5HW) and 7‐azatryptophan (7AW) are analogues of tryptophan that potentially can be incorporated biosynthetically into proteins and used as…”
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Fluorescence methods for studying equilibrium macromolecule-ligand interactions by Eftink, M R

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Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies by Eftink, M. R, Ghiron, C. A

“…Acrylamide is an efficient quencher of tryptophanyl fluorescence which we report to be very discriminating in sensing the degree of exposure of this residue in…”
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A multidimensional spectrophotometer for monitoring thermal unfolding transitions of macromolecules by Ramsay, G., Eftink, M.R.

“…We describe a multidimensional spectrometer that is capable of (nearly) simultaneous measurement of circular dichroism, steady-state fluorescence, and…”
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Exposure of tryptophanyl residues and protein dynamics by Eftink, M. R, Ghiron, C. A

“…The acrylamide quenching reaction is shown to be very discriminating in sensing the exposure of fluorescing tryptophanyl residues in globular proteins. The…”
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Frequency domain measurements of the fluorescence lifetime of ribonuclease T1 by Eftink, M.R., Ghiron, C.A.

“…Using multifrequency phase/modulation fluorometry, we have studied the fluorescence decay of the single tryptophan residue of ribonuclease T1 (RNase T1). At…”
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Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: general thermodynamic models and data for the binding of nucleotides to ribonuclease A by Eftink, Maurice R, Anusiem, A. C, Biltonen, Rodney L

“…General thermodynamic models are presented that can account for the existence of heat capacity changes and compensation between the enthalpy and entropy…”
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Effects of temperature on the fluorescence intensity and anisotropy decays of Staphylococcal nuclease and the less stable nuclease-conA-SG28 mutant by Eftink, Maurice R, Gryczynski, Ignacy, Wiczk, Wieslaw, Laczko, Gabor, Lakowicz, Joseph R

“…Frequency-domain fluorescence spectroscopy was used to investigate the effects of temperature on the intensity and anisotropy decays of the single tryptophan…”
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Local anesthetic-phospholipid interactions. Effects of ionic strength, temperature, and phospholipid mixtures on the binding of dibucaine to phospholipids by Barghouthi, S A, Puri, R K, Eftink, M R

“…The nature of the interaction of amphipathic drugs, such as dibucaine, with phospholipid bilayer membranes was investigated using equilibrium dialysis…”
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Indole fluorescence quenching studies on proteins and model systems: use of the inefficient quencher succinimide by Eftink, Maurice R, Ghiron, Camillo A

“…The author have compared the quenching of the fluorescence of proteins by acrylamide and succinimide, two chemically similar quenchers. they find that the…”
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Fluorescence studies of a local anesthetic-phospholipid interaction by Barghouthi, S, Eftink, M R

“…Steady-state and time-resolved fluorescence data are reported for the local anesthetic dibucaine in the absence and presence of phospholipid vesicles. These…”
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Dynamics of a Protein Matrix Revealed by Fluorescence Quenching by Eftink, M. R., Ghiron, C. A.

“…The fluorescence of the supposedly buried tryptophan in ribonuclease T1has been found to be collisionally quenched by acrylamide with a rate constant of 3 ×…”
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Fluorescence and conformational stability studies of Staphylococcus nuclease and its mutants, including the less stable nuclease-concanavalin A hybrids by Eftink, Maurice R, Ghiron, Camillo A, Kautz, Roger A, Fox, Robert O

“…We report steady-state and time-resolved fluorescence studies with the single tryptophan protein, Staphylococcus aureus A, and several of its site-directed…”
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Use of multiple spectroscopic methods to monitor equilibrium unfolding of proteins by Eftink, M R

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Acrylamide and oxygen fluorescence quenching studies with liver alcohol dehydrogenase using steady-state and phase fluorometry by Eftink, M. R, Jameson, D. M

“…The fluorescence lifetime of liver alcohol dehydrogenase (LADH) has been determined by phase fluorometry at various emission wavelengths and as a function of…”
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Reversible Thermal Unfolding of Ribonuclease T1 in Reverse Micelles by Shastry, M. C. R., Eftink, M. R.

“…The reverse micellar system formed by the negatively charged surfactant AOT and the organic solvent isooctane is used to solubilize the protein RNase T1. The…”
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Interaction of indoleacrylic acid with Trp aporepressor from Escherichia coli by Hu, D, Eftink, M R

“…Trans-beta-Indoleacrylic acid (IAA) binds with moderately high affinity to the dimeric protein, trp aporepressor from Escherichia coli. IAA is itself…”
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