Search Results - "Shrake, A"

Ligand-induced biphasic protein denaturation by SHRAKE, A, ROSS, P. D

“…The results of a thermodynamic calculation of the excess heat capacity that is based on experimental observations and that incorporates the effects of ligand…”
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Biphasic denaturation of human albumin due to ligand redistribution during unfolding by Shrake, A, Ross, P D

“…Denaturation of defatted human albumin monomer, monitored by differential scanning calorimetry, is monophasic as reflected by the single, resulting endotherm…”
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Decrease in stability of human albumin with increase in protein concentration by Ross, P D, Shrake, A

“…The stability (reflected in denaturation temperature, Td) of defatted human albumin monomer, monitored by differential scanning calorimetry, decreases with…”
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Environment and exposure to solvent of protein atoms. Lysozyme and insulin by Shrake, A, Rupley, J A

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Thermal stability of human albumin measured by differential scanning calorimetry. I. Effects of caprylate and N-acetyltryptophanate by Shrake, A, Finlayson, J S, Ross, P D

“…The thermal stability of 5% previously unheated, undefatted human albumin monomer in 145 mM Na+, pH 7.0 was investigated by differential scanning calorimetry…”
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Characterization of differences in isoelectric focusing behavior of alpha-proteinase inhibitor products by Marszal, Ewa, Shrake, Andrew

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On the binding of L-S- and L-R-diastereoisomers of the substrate analog L-methionine sulfoximine to glutamine synthetase from Escherichia coli by Shrake, A, Ginsburg, A, Wedler, F C, Sugiyama, Y

“…Active site ligand interactions with dodecameric glutamine synthetase from Escherichia coli were studied spectrally, using the resolved L-S- and…”
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A Novel Mode of Polymerization of alpha sub(1)-Proteinase Inhibitor by Marszal, E, Danino, D, Shrake, A

“…Patients homozygous for the Z mutant form of alpha sub(1)-proteinase inhibitor ( alpha sub(1)-PI) have an increased risk for the development of liver disease…”
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Calorimetric estimate of the enthalpy change for the substrate-promoted conformational transition of aspartate transcarbamoylase from Escherichia coli by Shrake, A, Ginsburg, A, Schachman, H K

“…Two different calorimetric methods are presented for estimating the enthalpy change of the substrate-promoted conformational transition of aspartate…”
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Conformational differences between unadenylylated and adenylylated glutamine synthetase from Escherichia coli on binding L-methionine sulfoximine by Shrake, A, Whitley, Jr, E J, Ginsburg, A

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Thermal stability of human albumin measured by differential scanning calorimetry. II. Effects of isomers of N-acetyltryptophanate and tryptophanate, pH, reheating, and dimerization by Ross, P D, Finlayson, J S, Shrake, A

“…Thermal stability of undefatted human albumin preparations at 5% concentration and neutral pH in 145 mM Na+ was investigated by differential scanning…”
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Optical properties of lysozyme. pH and saccharide binding difference spectra by Imoto, T, Andrews, L J, Banerjee, S K, Shrake, A, Forster, L S, Rupley, J A

“…Difference spectra associated with changes in pH and with binding of saccharides have been recorded for hen egg white (HEW) lysozyme, turkey egg white (TEW)…”
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The Folding of Alpha-1-Proteinase Inhibitor: Kinetic vs Equilibrium Control by Tran, Suong T., Shrake, Andrew

“…Previous folding studies of α-1-proteinase inhibitor (α1-PI), which regulates the activity of the serine protease human neutrophil elastase, show an…”
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Origins and consequences of ligand-induced multiphasic thermal protein denaturation by Shrake, A, Ross, P D

“…The presence of subsaturating levels of a high-affinity ligand has been demonstrated both by experiment and calculation to have far-reaching consequences on…”
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Partial unfolding of dodecameric glutamine synthetase from Escherichia coli: temperature-induced, reversible transitions of two domains by Shrake, Andrew, Fisher, Mark T, McFarland, Patrick J, Ginsburg, Ann

“…Glutamine synthetase (GS), Mr 622,000, from Escherichia coli contains 12 active sites formed at heterologous interfaces between subunits [Almassy, R. J.,…”
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Oxindolealanine-62 lysozyme: equilibrium calorimetric, and kinetic studies of the reaction with N-acetylglucosamine oligosaccharides by Shrake, Andrew, Rupley, John A

“…Oxindolealanine-62 lysozyme, formed by reaction with N-bromosuccinimide and purified by using affinity chromatography, was examined in its binding of…”
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Calorimetric studies on the binding of substrates and the inhibitor L-alanine to unadenylylated glutamine synthetase of Escherichia coli by Shrake, Andrew, Park, Robert, Ginsburg, Ann

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Calorimetric and equilibrium binding studies of the interaction of substrates with glutamine synthetase of Escherichia coli by Shrake, Andrew, Powers, Donald M, Ginsburg, Ann

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Purification of native and synthetic lysozyme with tri-(N-acetylglucosamine)-agarose by Cornelius, D A, Brown, W H, Shrake, A F, Rupley, J A

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