The Experts below are selected from a list of 116394 Experts worldwide ranked by ideXlab platform
Peter E M Candido - One of the best experts on this subject based on the ideXlab platform.
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microwave radiation can alter Protein Conformation without bulk heating
FEBS Letters, 2003Co-Authors: David I De Pomerai, Brette Smith, Adam Dawe, Kate North, Tim Smith, David B Archer, Ian R Duce, D Jones, Peter E M CandidoAbstract:Exposure to microwave radiation enhances the aggregation of bovine serum albumin in vitro in a time- and temperature-dependent manner. Microwave radiation also promotes amyloid fibril formation by bovine insulin at 60°C. These alterations in Protein Conformation are not accompanied by measurable temperature changes, consistent with estimates from field modelling of the specific absorbed radiation (15–20 mW kg−1). Limited denaturation of cellular Proteins could explain our previous observation that modest heat-shock responses are induced by microwave exposure in Caenorhabditis elegans. We also show that heat-shock responses both to heat and microwaves are suppressed after RNA interference ablating heat-shock factor function.
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microwave radiation can alter Protein Conformation without bulk heating
FEBS Letters, 2003Co-Authors: David I De Pomerai, Brette Smith, Adam Dawe, Kate North, David B Archer, Ian R Duce, D Jones, Timothy P L Smith, Peter E M CandidoAbstract:Exposure to microwave radiation enhances the aggregation of bovine serum albumin in vitro in a time- and temperature-dependent manner. Microwave radiation also promotes amyloid fibril formation by bovine insulin at 60 degrees C. These alterations in Protein Conformation are not accompanied by measurable temperature changes, consistent with estimates from field modelling of the specific absorbed radiation (15-20 mW kg(-1)). Limited denaturation of cellular Proteins could explain our previous observation that modest heat-shock responses are induced by microwave exposure in Caenorhabditis elegans. We also show that heat-shock responses both to heat and microwaves are suppressed after RNA interference ablating heat-shock factor function.
Vasanthy Narayanaswami - One of the best experts on this subject based on the ideXlab platform.
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pyrene a probe to study Protein Conformation and Conformational changes
Molecules, 2011Co-Authors: Gursharan K Bains, Arti B Patel, Vasanthy NarayanaswamiAbstract:The review focuses on the unique spectral features of pyrene that can be utilized to investigate Protein structure and Conformation. Pyrene is a fluorescent probe that can be attached covalently to Protein side chains, such as sulfhydryl groups. The spectral features of pyrene are exquisitely sensitive to the microenvironment of the probe: it exhibits an ensemble of monomer fluorescence emission peaks that report on the polarity of the probe microenvironment, and an additional band at longer wavelengths, the appearance of which reflects the presence of another pyrene molecule in spatial proximity (~10 A). Its high extinction coefficient allows us to study labeled Proteins in solution at physiologically relevant concentrations. The environmentally- and spatially-sensitive features of pyrene allow monitoring Protein Conformation, Conformational changes, Protein folding and unfolding, Protein-Protein, Protein-lipid and Protein-membrane interactions.
Jeffrey Robbins - One of the best experts on this subject based on the ideXlab platform.
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Protein Conformation–Based Disease: Getting to the Heart of the Matter
Annual review of physiology, 2010Co-Authors: David Terrell, Jeffrey RobbinsAbstract:Introduction The topics presented in the Cardiovascular Physiology section of this volume highlight exciting developments in our understanding of Protein Conformation–based disease. The disease models created over the past decade by precise genetic manipulation provide a set of powerful tools to explore primary, secondary, and tertiary pathways that might underlie development of clinically important pathologies.
Mordechai Sheves - One of the best experts on this subject based on the ideXlab platform.
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Protein Conformational alterations induced by the retinal excited state in proton and sodium pumping rhodopsins.
Physical chemistry chemical physics : PCCP, 2019Co-Authors: Mihir Ghosh, Kwang-hwan Jung, Mordechai ShevesAbstract:Retinal Proteins’ biological activity is triggered by the retinal chromophore's light absorption, which initiates a photocycle. However, the mechanism by which retinal light excitation induces the Protein's response is not completely understood. Recently, two new retinal Proteins were discovered, namely, King Sejong 1-2 (KS1-2) and Nonlabens (Donghaeana) dokdonensis (DDR2), which exhibit H+ and Na+ pumping activities, respectively. To pinpoint whether Protein Conformation alterations can be achieved without light-induced retinal C13C14 double-bond isomerization, we utilized the hydroxylamine reaction, which cleaves the protonated Schiff base bond through which the retinal chromophore is covalently bound to the Protein. The reaction is accelerated by light even though the cleavage is not a photochemical reaction. Therefore, the cleavage reaction may serve as a tool to detect Protein Conformation alterations. We discovered that in both KS1-2 and DDR2, the hydroxylamine reaction is light accelerated, even in artificial pigments derived from synthetic retinal in which the crucial C13C14 double-bond isomerization is prevented. Therefore, we propose that in both Proteins the light-induced retinal charge redistribution taking place in the retinal excited state polarizes the Protein, which, in turn, triggers Protein Conformation alterations. A further general possible application of the present finding is associated with other photoreceptor Proteins having retinal or other non-retinal chromophores whose light excitation may affect the Protein Conformation.
Gary D. Fullerton - One of the best experts on this subject based on the ideXlab platform.
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Role of Protein Conformation and aggregation in pumping water in and out of a cell.
Cell biology international, 2005Co-Authors: Ivan L. Cameron, Kalpana M. Kanal, Gary D. FullertonAbstract:Dialysis cassettes containing BSA solutions were used to simulate passive in vivo conditions to assess the effect of Protein Conformation and aggregation on cell water content. The cassettes were suspended in dextran solutions to provide a range of fixed osmotic stress values simulating blood plasma. The system was placed on a shaker for 24 h to attain equilibrium. Four manipulation methods; pH, cosolute salt concentration, e.g. NaCl, temperature annealing and urea concentration denaturant were varied to produce well-known manipulations of BSA Conformation. It was observed that the cell water content varied from +14% to about -13% with changes in Protein Conformation and aggregation. The findings demonstrate that a change in Protein Conformation and aggregation, pumps water in and out of a cell to maintain equilibrium % water content matching the Protein Conformational hydration parameter. This concept supplements existing theories on cell volume regulation.
