The Experts below are selected from a list of 30426 Experts worldwide ranked by ideXlab platform
Subrata Mukhopadhyay - One of the best experts on this subject based on the ideXlab platform.
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thermodynamic study of rhodamine 123 calf thymus dna interaction determination of calorimetric enthalpy by optical melting study
Journal of Physical Chemistry B, 2014Co-Authors: Abdulla Al Masum, Maharudra Chakraborty, Prateek Pandya, Umesh Chandra Halder, Md Maidul Islam, Subrata MukhopadhyayAbstract:In this paper, the interaction of rhodamine123 (R123) with calf thymus DNA has been studied using molecular modeling and other Biophysical Methods like UV–vis spectroscopy, fluoremetry, optical melting, isothermal titration calorimetry, and circular dichroic studies. Results showed that the binding energy is about −6 to −8 kcal/mol, and the binding process is favored by both negative enthalpy change and positive entropy change. A new method to determine different thermodynamic properties like calorimetric enthalpy and heat capacity change has been introduced in this paper. The obtained data has been crossed-checked by other Methods. After dissecting the free-energy contribution, it was observed that the binding was favored by both negative hydrophobic free energy and negative molecular free energy which compensated for the positive free energies due to the conformational change loss of rotational and transitional freedom of the DNA helix.
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thermodynamic study of rhodamine 123 calf thymus dna interaction determination of calorimetric enthalpy by optical melting study b
The Journal of Physical Chemistry, 2014Co-Authors: Abdulla Al Masum, Maharudra Chakraborty, Prateek Pandya, Umesh Chandra Halder, Md Maidul Islam, Subrata MukhopadhyayAbstract:In this paper, the interaction of rhodamine123 (R123) with calf thymus DNA has been studied using molecular modeling and other Biophysical Methods like UV–vis spectroscopy, fluoremetry, optical melting, isothermal titration calorimetry, and circular dichroic studies. Results showed that the binding energy is about −6 to −8 kcal/mol, and the binding process is favored by both negative enthalpy change and positive entropy change. A new method to determine different thermodynamic properties like calorimetric enthalpy and heat capacity change has been introduced in this paper. The obtained data has been crossed-checked by other Methods. After dissecting the free-energy contribution, it was observed that the binding was favored by both negative hydrophobic free energy and negative molecular free energy which compensated for the positive free energies due to the conformational change loss of rotational and transitional freedom of the DNA helix.
Daniel Mayer - One of the best experts on this subject based on the ideXlab platform.
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distinct g protein coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation
Nature Communications, 2019Co-Authors: Daniel Mayer, Fred F Damberger, Mamidi Samarasimhareddy, Miki Feldmueller, Ziva Vuckovic, Tilman FlockAbstract:Cellular functions of arrestins are determined in part by the pattern of phosphorylation on the G protein-coupled receptors (GPCRs) to which arrestins bind. Despite high-resolution structural data of arrestins bound to phosphorylated receptor C-termini, the functional role of each phosphorylation site remains obscure. Here, we employ a library of synthetic phosphopeptide analogues of the GPCR rhodopsin C-terminus and determine the ability of these peptides to bind and activate arrestins using a variety of biochemical and Biophysical Methods. We further characterize how these peptides modulate the conformation of arrestin-1 by nuclear magnetic resonance (NMR). Our results indicate different functional classes of phosphorylation sites: ‘key sites’ required for arrestin binding and activation, an ‘inhibitory site’ that abrogates arrestin binding, and ‘modulator sites’ that influence the global conformation of arrestin. These functional motifs allow a better understanding of how different GPCR phosphorylation patterns might control how arrestin functions in the cell. The cellular functions of arrestins are determined in part by the pattern of phosphorylation on the G protein-coupled receptors (GPCRs) to which arrestins bind. Here, authors use a library of synthetic phosphopeptide analogues of the GPCR rhodopsin C-terminus and determine the ability of these peptides to bind and activate arrestins using a variety of biochemical and Biophysical Methods.
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Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation
Nature Publishing Group, 2019Co-Authors: Daniel Mayer, Fred F Damberger, Mamidi Samarasimhareddy, Miki Feldmueller, Ziva Vuckovic, Tilman Flock, Brian Bauer, Eshita Mutt, Franziska Zosel, Frédéric H. T. AllainAbstract:The cellular functions of arrestins are determined in part by the pattern of phosphorylation on the G protein-coupled receptors (GPCRs) to which arrestins bind. Here, authors use a library of synthetic phosphopeptide analogues of the GPCR rhodopsin C-terminus and determine the ability of these peptides to bind and activate arrestins using a variety of biochemical and Biophysical Methods
Abdulla Al Masum - One of the best experts on this subject based on the ideXlab platform.
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thermodynamic study of rhodamine 123 calf thymus dna interaction determination of calorimetric enthalpy by optical melting study
Journal of Physical Chemistry B, 2014Co-Authors: Abdulla Al Masum, Maharudra Chakraborty, Prateek Pandya, Umesh Chandra Halder, Md Maidul Islam, Subrata MukhopadhyayAbstract:In this paper, the interaction of rhodamine123 (R123) with calf thymus DNA has been studied using molecular modeling and other Biophysical Methods like UV–vis spectroscopy, fluoremetry, optical melting, isothermal titration calorimetry, and circular dichroic studies. Results showed that the binding energy is about −6 to −8 kcal/mol, and the binding process is favored by both negative enthalpy change and positive entropy change. A new method to determine different thermodynamic properties like calorimetric enthalpy and heat capacity change has been introduced in this paper. The obtained data has been crossed-checked by other Methods. After dissecting the free-energy contribution, it was observed that the binding was favored by both negative hydrophobic free energy and negative molecular free energy which compensated for the positive free energies due to the conformational change loss of rotational and transitional freedom of the DNA helix.
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thermodynamic study of rhodamine 123 calf thymus dna interaction determination of calorimetric enthalpy by optical melting study b
The Journal of Physical Chemistry, 2014Co-Authors: Abdulla Al Masum, Maharudra Chakraborty, Prateek Pandya, Umesh Chandra Halder, Md Maidul Islam, Subrata MukhopadhyayAbstract:In this paper, the interaction of rhodamine123 (R123) with calf thymus DNA has been studied using molecular modeling and other Biophysical Methods like UV–vis spectroscopy, fluoremetry, optical melting, isothermal titration calorimetry, and circular dichroic studies. Results showed that the binding energy is about −6 to −8 kcal/mol, and the binding process is favored by both negative enthalpy change and positive entropy change. A new method to determine different thermodynamic properties like calorimetric enthalpy and heat capacity change has been introduced in this paper. The obtained data has been crossed-checked by other Methods. After dissecting the free-energy contribution, it was observed that the binding was favored by both negative hydrophobic free energy and negative molecular free energy which compensated for the positive free energies due to the conformational change loss of rotational and transitional freedom of the DNA helix.
Tilman Flock - One of the best experts on this subject based on the ideXlab platform.
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distinct g protein coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation
Nature Communications, 2019Co-Authors: Daniel Mayer, Fred F Damberger, Mamidi Samarasimhareddy, Miki Feldmueller, Ziva Vuckovic, Tilman FlockAbstract:Cellular functions of arrestins are determined in part by the pattern of phosphorylation on the G protein-coupled receptors (GPCRs) to which arrestins bind. Despite high-resolution structural data of arrestins bound to phosphorylated receptor C-termini, the functional role of each phosphorylation site remains obscure. Here, we employ a library of synthetic phosphopeptide analogues of the GPCR rhodopsin C-terminus and determine the ability of these peptides to bind and activate arrestins using a variety of biochemical and Biophysical Methods. We further characterize how these peptides modulate the conformation of arrestin-1 by nuclear magnetic resonance (NMR). Our results indicate different functional classes of phosphorylation sites: ‘key sites’ required for arrestin binding and activation, an ‘inhibitory site’ that abrogates arrestin binding, and ‘modulator sites’ that influence the global conformation of arrestin. These functional motifs allow a better understanding of how different GPCR phosphorylation patterns might control how arrestin functions in the cell. The cellular functions of arrestins are determined in part by the pattern of phosphorylation on the G protein-coupled receptors (GPCRs) to which arrestins bind. Here, authors use a library of synthetic phosphopeptide analogues of the GPCR rhodopsin C-terminus and determine the ability of these peptides to bind and activate arrestins using a variety of biochemical and Biophysical Methods.
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Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation
Nature Publishing Group, 2019Co-Authors: Daniel Mayer, Fred F Damberger, Mamidi Samarasimhareddy, Miki Feldmueller, Ziva Vuckovic, Tilman Flock, Brian Bauer, Eshita Mutt, Franziska Zosel, Frédéric H. T. AllainAbstract:The cellular functions of arrestins are determined in part by the pattern of phosphorylation on the G protein-coupled receptors (GPCRs) to which arrestins bind. Here, authors use a library of synthetic phosphopeptide analogues of the GPCR rhodopsin C-terminus and determine the ability of these peptides to bind and activate arrestins using a variety of biochemical and Biophysical Methods
Maharudra Chakraborty - One of the best experts on this subject based on the ideXlab platform.
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thermodynamic study of rhodamine 123 calf thymus dna interaction determination of calorimetric enthalpy by optical melting study
Journal of Physical Chemistry B, 2014Co-Authors: Abdulla Al Masum, Maharudra Chakraborty, Prateek Pandya, Umesh Chandra Halder, Md Maidul Islam, Subrata MukhopadhyayAbstract:In this paper, the interaction of rhodamine123 (R123) with calf thymus DNA has been studied using molecular modeling and other Biophysical Methods like UV–vis spectroscopy, fluoremetry, optical melting, isothermal titration calorimetry, and circular dichroic studies. Results showed that the binding energy is about −6 to −8 kcal/mol, and the binding process is favored by both negative enthalpy change and positive entropy change. A new method to determine different thermodynamic properties like calorimetric enthalpy and heat capacity change has been introduced in this paper. The obtained data has been crossed-checked by other Methods. After dissecting the free-energy contribution, it was observed that the binding was favored by both negative hydrophobic free energy and negative molecular free energy which compensated for the positive free energies due to the conformational change loss of rotational and transitional freedom of the DNA helix.
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thermodynamic study of rhodamine 123 calf thymus dna interaction determination of calorimetric enthalpy by optical melting study b
The Journal of Physical Chemistry, 2014Co-Authors: Abdulla Al Masum, Maharudra Chakraborty, Prateek Pandya, Umesh Chandra Halder, Md Maidul Islam, Subrata MukhopadhyayAbstract:In this paper, the interaction of rhodamine123 (R123) with calf thymus DNA has been studied using molecular modeling and other Biophysical Methods like UV–vis spectroscopy, fluoremetry, optical melting, isothermal titration calorimetry, and circular dichroic studies. Results showed that the binding energy is about −6 to −8 kcal/mol, and the binding process is favored by both negative enthalpy change and positive entropy change. A new method to determine different thermodynamic properties like calorimetric enthalpy and heat capacity change has been introduced in this paper. The obtained data has been crossed-checked by other Methods. After dissecting the free-energy contribution, it was observed that the binding was favored by both negative hydrophobic free energy and negative molecular free energy which compensated for the positive free energies due to the conformational change loss of rotational and transitional freedom of the DNA helix.