Relative stability of the α‐helix of deuterated poly(γ‐benzyl‐<scp>L</scp>‐glutamate)

Karasz, Frank E.; Gajnos, G. E.

doi:10.1002/bip.1976.360151006

Cited by 10 publications

(2 citation statements)

References 15 publications

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“…In addition, they examined the effects of D 2 O on actin polymerization in vitro and demonstrated that D 2 O accelerates purified globular actin polymerization immediately upon exposure to D 2 O, whereas the total amount of polymerized actin later during treatment with D 2 O is the same as that in H 2 O. Therefore, one possible mechanism underlying D 2 O-induced actin filament redistribution may involve the hydrogen to deuterium exchange in globular proteins (Hermans and Scheraga, 1959;Scheraga, 1960), which results in more stable protein structures (Sing and Wood, 1969;Karasz and Gajnos, 1976), and thus is caused by a typical isotope exchange effect.…”

Section: Cellular Responses Under D 2 O Exposurementioning

confidence: 99%

Hydrogen-Deuterium Exchange Effects on β-Endorphin Release from AtT20 Murine Pituitary Tumor Cells

Ikeda

Suzuki

Kishio

et al. 2004

Biophysical Journal

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Abundant evidences demonstrate that deuterium oxide (D2O) modulates various secretory activities, but specific mechanisms remain unclear. Using AtT20 cells, we examined effects of D2O on physiological processes underlying beta-endorphin release. Immunofluorescent confocal microscopy demonstrated that 90% D2O buffer increased the amount of actin filament in cell somas and decreased it in cell processes, whereas beta-tubulin was not affected. Ca2+ imaging demonstrated that high-K+-induced Ca2+ influx was not affected during D2O treatment, but was completely inhibited upon D2O washout. The H2O/D2O replacement in internal solutions of patch electrodes reduced Ca2+ currents evoked by depolarizing voltage steps, whereas additional extracellular H2O/D2O replacement recovered the currents, suggesting that D2O gradient across plasma membrane is critical for Ca2+ channel kinetics. Radioimmunoassay of high-K+-induced beta-endorphin release demonstrated an increase during D2O treatment and a decrease upon D(2)O washout. These results demonstrate that the H2O-to-D2O-induced increase in beta-endorphin release corresponded with the redistribution of actin, and the D2O-to-H2O-induced decrease in beta-endorphin release corresponded with the inhibition of voltage-sensitive Ca2+ channels. The computer modeling suggests that the differences in the zero-point vibrational energy between protonated and deuterated amino acids produce an asymmetric distribution of these amino acids upon D2O washout and this causes the dysfunction of Ca2+ channels.

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Section: Cellular Responses Under D 2 O Exposurementioning

confidence: 99%

Hydrogen-Deuterium Exchange Effects on β-Endorphin Release from AtT20 Murine Pituitary Tumor Cells

Ikeda

Suzuki

Kishio

et al. 2004

Biophysical Journal

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“…They concluded that alteration of stress fibres in cultured cells may be caused by a direct effect of D 2 O on cellular microfilament dynamics (Omori et al, 1997). One possible mechanism underling D 2 O-induced actin filament redistribution may involve H to D exchange in globular protein (Hermans & Scheraga, 1959;Scheraga, 1960), which results in a more stable protein structure (Karasz & Gajnos, 1976;Sing & Wood, 1976).…”

Section: Effect Of D 2 O On the Actin Structurementioning

confidence: 99%

Functional Difference Between Deuterated and Protonated Macromolecules

Sugiyama¹,

Yoshioka²

2012

Protein Structure

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Differences in structure and stability between normal and deuterated proteins (phycocyanin)

et al. 1983

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SynopsisDifferential scanning microcalorimetry was used to investigate the enthalpy ( A H d ) and the temperature (td) of thermal denaturation of normal and deuterated phycocyanins isolated from two blue-green algae, Plectonerna calothrieoides and Phwmidium luridurn. Values of td in deuterated proteins are about 5°C lower than those in normat proteins. The magnitudes of A H d in deuterated proteins are 1%36% lower than in normal proteins. The heatcapacity change (AC,) in protein unfolding is essentially the same (2 kcal/mol/K) for deuterated and normal proteins within the experimental error. A t close to physiological temperature (27"C), the differences in thermodynamic functions in the native and denatured states are much higher in normal proteins than in deuterated proteins. CD was employed to evaluate both the secondary structures and urea denaturation of these two types of proteins. In P. luridurn, deuterated protein is about 8% higher in a-helix content; in P. calothricoides it is not significantly higher. Deuterated proteins are less resistant to the denaturant urea than are normal proteins: the denaturant concentration at the midpoint of the denaturation curve is 0.6-1.2 mol/L lower in the deuterated proteins. The apparent free energies of unfolding of deuterated proteins at zero denaturant concentration are 1.1-1.5 kcal/mol less than for normal proteins.

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Relative stability of the α‐helix of deuterated poly(γ‐benzyl‐L‐glutamate)

Cited by 10 publications

References 15 publications

Hydrogen-Deuterium Exchange Effects on β-Endorphin Release from AtT20 Murine Pituitary Tumor Cells

Hydrogen-Deuterium Exchange Effects on β-Endorphin Release from AtT20 Murine Pituitary Tumor Cells

Functional Difference Between Deuterated and Protonated Macromolecules

Differences in structure and stability between normal and deuterated proteins (phycocyanin)

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