Probing of the microwave radiation effect on the green fluorescent protein luminescence in solution

Copty, A.; Sakran, F.; Popov, O. E.; Ziblat, Roy; Danieli, Tsafi; Golosovsky, M.; Davidov, D.

doi:10.1016/j.synthmet.2005.09.028

Cited by 16 publications

(14 citation statements)

References 11 publications

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“…28 Several studies suggest that microwaves induce structural rearrangements of proteins not related to the temperature. 29,30 In organic synthesis the thermal and non-thermal microwave effects are still being debated. 31,32 The idea of studying the effects of individual degrees of freedom is appealing for many reasons.…”

Section: Introductionmentioning

confidence: 99%

Effects of the translational and rotational degrees of freedom on the hydration of simple solutes

Mohorič

Hribar-Lee

Vlachy

2014

The Journal of Chemical Physics

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Molecular dynamics simulations with separate thermostats for rotational and translational motion were used to study the effect of these degrees of freedom on the structure of water around model solutes. To describe water molecules we used the SPC/E model. The simplest solute studied here, the hydrophobe, was represented as a Lennard-Jones particle. Since direct interaction between the hydrophobe and water molecules has no angular dependence the influence of the increase of the rotational temperature on the solvation of a hydrophobe is only indirect. In the next step the central solute was assumed to be charged with either a positive or a negative charge to mimic an ion in water. Hence, depending on the charge of the ion, the neighboring water molecules assumed different angular distributions. The principal conclusions of this work are: (i) an increase of the translational temperature always decreases the height of the first peak in the solute-water radial distribution function; (ii) an increase of the rotational temperature yields an increase in the first peak in the solute-water radial distribution function for hydrophobes and cations; (iii) in contrast to this, the solvation peak decreases around ions with sufficiently large negative charge; and (iv) an increase of the rotational temperature affects cations in an opposite way to anions. For this reason complex molecules with a small net charge may not be very sensitive to variation of the rotational temperature. © 2014 AIP Publishing LLC. [http://dx

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Section: Introductionmentioning

confidence: 99%

Effects of the translational and rotational degrees of freedom on the hydration of simple solutes

Mohorič

Hribar-Lee

Vlachy

2014

The Journal of Chemical Physics

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“…Evidence has been presented [Bohr and Bohr, 2000a,b;Copty et al, 2005] that the effect of microwaves on protein conformation and function is not the same as the effects of ambient heating with conducted heat, at the same temperature. In the work of Bohr and Bohr, the effect of microwaves on a cold denaturing protein was studied.…”

Section: Introductionmentioning

confidence: 99%

“…This is contrary to the effects of heating in thermodynamic equilibrium which would promote refolding in both cases. In the work of Copty et al [2005] it was found that the effects of microwaves on the fluorescence of a green fluorescent protein was greater than could be explained on the basis of the temperature changes alone.…”

Section: Introductionmentioning

confidence: 99%

Non‐Thermal effects in the microwave induced unfolding of proteins observed by chaperone binding

George

Bilek

McKenzie

2008

Bioelectromagnetics

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We study the effect of microwaves at 2,450 MHz on protein unfolding using surface plasmon resonance sensing. Our experimental method makes use of the fact that unfolding proteins tend to bind to chaperones on their unfolding pathway and this attachment is readily monitored by surface plasmon resonance. We use the protein citrate synthase (CS) for this study as it shows strong binding to the chaperone alpha crystallin when stressed by exposure to excess temperature. The results of microwave heating are compared with the effect of ambient heating and a combination of ambient and microwave heating to the same final temperature. We study the temperature distributions during the heating process. We show that microwaves cause a significantly higher degree of unfolding than conventional thermal stress for protein solutions heated to the same maximum temperature.

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“…The functionality of the nanoheater for single molecule studies will later on be tested using the relatively well known temperature dependence of the GFP protein [17]. As for positioning molecules on the wires, this could be performed with similar techniques as in the case of nanocrystals.…”

Section: Discussionmentioning

confidence: 99%

Assembly of CdSe/ZnS nanocrystals on microwires and nanowires for temperature sensing

Löw

Pioufle

Kim

et al. 2008

Sensors and Actuators B: Chemical

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Probing of the microwave radiation effect on the green fluorescent protein luminescence in solution

Cited by 16 publications

References 11 publications

Effects of the translational and rotational degrees of freedom on the hydration of simple solutes

Effects of the translational and rotational degrees of freedom on the hydration of simple solutes

Non‐Thermal effects in the microwave induced unfolding of proteins observed by chaperone binding

Assembly of CdSe/ZnS nanocrystals on microwires and nanowires for temperature sensing

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