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Daniel Kmiecik - One of the best experts on this subject based on the ideXlab platform.
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energy transfer studies between trp Residues of three lipocalin proteins family α1 acid glycoprotein orosomucoid β lactoglobulin and porcine odorant binding protein and the fluorescent probe 1 aminoanthracene 1 ama
Journal of Fluorescence, 2015Co-Authors: Jihad René Albani, Loic Bretesche, Julie Vogelaer, Daniel KmiecikAbstract:Energy transfer studies between Trp Residues of α1-acid glycoprotein, β-lactoglobulin and porcine odorant binding protein (OBP) and the fluorescent probe 1-aminoanthracene (1-AMA) were performed. 1-AMA binds to the hydrophobic binding sites of the three proteins inducing a decrease in the fluorescence intensity of the Trp Residues accompanied by an increase of that of 1-AMA. Our results indicate that 1-AMA is in close contact with hydrophobic Tryptophan Residue of β-lactoglobulin (Trp 19) to the difference of its binding to OBP, where Trp Residues are far from the pocket and to α1-acid glycoprotein where three Trp Residues are present at different areas of the protein.
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energy transfer studies between trp Residues of three lipocalin proteins family α1 acid glycoprotein orosomucoid β lactoglobulin and porcine odorant binding protein and the fluorescent probe 1 aminoanthracene 1 ama
Journal of Fluorescence, 2015Co-Authors: Jihad René Albani, Loic Bretesche, Julie Vogelaer, Daniel KmiecikAbstract:Energy transfer studies between Trp Residues of α(1)-acid glycoprotein, β-lactoglobulin and porcine odorant binding protein (OBP) and the fluorescent probe 1-aminoanthracene (1-AMA) were performed. 1-AMA binds to the hydrophobic binding sites of the three proteins inducing a decrease in the fluorescence intensity of the Trp Residues accompanied by an increase of that of 1-AMA. Our results indicate that 1-AMA is in close contact with hydrophobic Tryptophan Residue of β-lactoglobulin (Trp 19) to the difference of its binding to OBP, where Trp Residues are far from the pocket and to α(1)-acid glycoprotein where three Trp Residues are present at different areas of the protein.
Jihad René Albani - One of the best experts on this subject based on the ideXlab platform.
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energy transfer studies between trp Residues of three lipocalin proteins family α1 acid glycoprotein orosomucoid β lactoglobulin and porcine odorant binding protein and the fluorescent probe 1 aminoanthracene 1 ama
Journal of Fluorescence, 2015Co-Authors: Jihad René Albani, Loic Bretesche, Julie Vogelaer, Daniel KmiecikAbstract:Energy transfer studies between Trp Residues of α1-acid glycoprotein, β-lactoglobulin and porcine odorant binding protein (OBP) and the fluorescent probe 1-aminoanthracene (1-AMA) were performed. 1-AMA binds to the hydrophobic binding sites of the three proteins inducing a decrease in the fluorescence intensity of the Trp Residues accompanied by an increase of that of 1-AMA. Our results indicate that 1-AMA is in close contact with hydrophobic Tryptophan Residue of β-lactoglobulin (Trp 19) to the difference of its binding to OBP, where Trp Residues are far from the pocket and to α1-acid glycoprotein where three Trp Residues are present at different areas of the protein.
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energy transfer studies between trp Residues of three lipocalin proteins family α1 acid glycoprotein orosomucoid β lactoglobulin and porcine odorant binding protein and the fluorescent probe 1 aminoanthracene 1 ama
Journal of Fluorescence, 2015Co-Authors: Jihad René Albani, Loic Bretesche, Julie Vogelaer, Daniel KmiecikAbstract:Energy transfer studies between Trp Residues of α(1)-acid glycoprotein, β-lactoglobulin and porcine odorant binding protein (OBP) and the fluorescent probe 1-aminoanthracene (1-AMA) were performed. 1-AMA binds to the hydrophobic binding sites of the three proteins inducing a decrease in the fluorescence intensity of the Trp Residues accompanied by an increase of that of 1-AMA. Our results indicate that 1-AMA is in close contact with hydrophobic Tryptophan Residue of β-lactoglobulin (Trp 19) to the difference of its binding to OBP, where Trp Residues are far from the pocket and to α(1)-acid glycoprotein where three Trp Residues are present at different areas of the protein.
Julie Vogelaer - One of the best experts on this subject based on the ideXlab platform.
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energy transfer studies between trp Residues of three lipocalin proteins family α1 acid glycoprotein orosomucoid β lactoglobulin and porcine odorant binding protein and the fluorescent probe 1 aminoanthracene 1 ama
Journal of Fluorescence, 2015Co-Authors: Jihad René Albani, Loic Bretesche, Julie Vogelaer, Daniel KmiecikAbstract:Energy transfer studies between Trp Residues of α1-acid glycoprotein, β-lactoglobulin and porcine odorant binding protein (OBP) and the fluorescent probe 1-aminoanthracene (1-AMA) were performed. 1-AMA binds to the hydrophobic binding sites of the three proteins inducing a decrease in the fluorescence intensity of the Trp Residues accompanied by an increase of that of 1-AMA. Our results indicate that 1-AMA is in close contact with hydrophobic Tryptophan Residue of β-lactoglobulin (Trp 19) to the difference of its binding to OBP, where Trp Residues are far from the pocket and to α1-acid glycoprotein where three Trp Residues are present at different areas of the protein.
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energy transfer studies between trp Residues of three lipocalin proteins family α1 acid glycoprotein orosomucoid β lactoglobulin and porcine odorant binding protein and the fluorescent probe 1 aminoanthracene 1 ama
Journal of Fluorescence, 2015Co-Authors: Jihad René Albani, Loic Bretesche, Julie Vogelaer, Daniel KmiecikAbstract:Energy transfer studies between Trp Residues of α(1)-acid glycoprotein, β-lactoglobulin and porcine odorant binding protein (OBP) and the fluorescent probe 1-aminoanthracene (1-AMA) were performed. 1-AMA binds to the hydrophobic binding sites of the three proteins inducing a decrease in the fluorescence intensity of the Trp Residues accompanied by an increase of that of 1-AMA. Our results indicate that 1-AMA is in close contact with hydrophobic Tryptophan Residue of β-lactoglobulin (Trp 19) to the difference of its binding to OBP, where Trp Residues are far from the pocket and to α(1)-acid glycoprotein where three Trp Residues are present at different areas of the protein.
Loic Bretesche - One of the best experts on this subject based on the ideXlab platform.
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energy transfer studies between trp Residues of three lipocalin proteins family α1 acid glycoprotein orosomucoid β lactoglobulin and porcine odorant binding protein and the fluorescent probe 1 aminoanthracene 1 ama
Journal of Fluorescence, 2015Co-Authors: Jihad René Albani, Loic Bretesche, Julie Vogelaer, Daniel KmiecikAbstract:Energy transfer studies between Trp Residues of α1-acid glycoprotein, β-lactoglobulin and porcine odorant binding protein (OBP) and the fluorescent probe 1-aminoanthracene (1-AMA) were performed. 1-AMA binds to the hydrophobic binding sites of the three proteins inducing a decrease in the fluorescence intensity of the Trp Residues accompanied by an increase of that of 1-AMA. Our results indicate that 1-AMA is in close contact with hydrophobic Tryptophan Residue of β-lactoglobulin (Trp 19) to the difference of its binding to OBP, where Trp Residues are far from the pocket and to α1-acid glycoprotein where three Trp Residues are present at different areas of the protein.
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energy transfer studies between trp Residues of three lipocalin proteins family α1 acid glycoprotein orosomucoid β lactoglobulin and porcine odorant binding protein and the fluorescent probe 1 aminoanthracene 1 ama
Journal of Fluorescence, 2015Co-Authors: Jihad René Albani, Loic Bretesche, Julie Vogelaer, Daniel KmiecikAbstract:Energy transfer studies between Trp Residues of α(1)-acid glycoprotein, β-lactoglobulin and porcine odorant binding protein (OBP) and the fluorescent probe 1-aminoanthracene (1-AMA) were performed. 1-AMA binds to the hydrophobic binding sites of the three proteins inducing a decrease in the fluorescence intensity of the Trp Residues accompanied by an increase of that of 1-AMA. Our results indicate that 1-AMA is in close contact with hydrophobic Tryptophan Residue of β-lactoglobulin (Trp 19) to the difference of its binding to OBP, where Trp Residues are far from the pocket and to α(1)-acid glycoprotein where three Trp Residues are present at different areas of the protein.
Jozsef Orban - One of the best experts on this subject based on the ideXlab platform.
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Functional dynamics of a single Tryptophan Residue in a BLUF protein revealed by fluorescence spectroscopy
Scientific Reports, 2020Co-Authors: Kristof Karadi, Sofia Kapetanaki, Katalin Raics, Ildiko Pecsi, Robert Kapronczai, Zsuzsanna Fekete, James Iuliano, Jinnette Tolentino Collado, Agnieszka Gil, Jozsef OrbanAbstract:Blue Light Using flavin (BLUf) domains are increasingly being adopted for use in optogenetic constructs. Despite this, much remains to be resolved on the mechanism of their activation. The advent of unnatural amino acid mutagenesis opens up a new toolbox for the study of protein structural dynamics. The Tryptophan analogue, 7-aza-Trp (7AW) was incorporated in the BLUF domain of the Activation of Photopigment and pucA (AppA) photoreceptor in order to investigate the functional dynamics of the crucial W104 Residue during photoactivation of the protein. The 7-aza modification to Trp makes selective excitation possible using 310 nm excitation and 380 nm emission, separating the signals of interest from other Trp and Tyr Residues. We used Förster energy transfer (FRET) between 7AW and the flavin to estimate the distance between Trp and flavin in both the light-and darkadapted states in solution. Nanosecond fluorescence anisotropy decay and picosecond fluorescence lifetime measurements for the flavin revealed a rather dynamic picture for the Tryptophan Residue. In the dark-adapted state, the major population of W104 is pointing away from the flavin and can move freely, in contrast to previous results reported in the literature. Upon blue-light excitation, the dominant Tryptophan population is reorganized, moves closer to the flavin occupying a rigidly bound state participating in the hydrogen-bond network around the flavin molecule.
