The Experts below are selected from a list of 163050 Experts worldwide ranked by ideXlab platform
Zhijian Cao - One of the best experts on this subject based on the ideXlab platform.
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Extreme diversity of scorpion venom Peptides and Proteins revealed by transcriptomic analysis: Implication for proteome evolution of scorpion venom arsenal
Journal of Proteomics, 2012Co-Authors: Ruiming Zhao, Zhijian CaoAbstract:Venom is an important genetic development crucial to the survival of scorpions for over 400 million years. We studied the evolution of the scorpion venom arsenal by means of comparative transcriptome analysis of venom glands and phylogenetic analysis of shared types of venom Peptides and Proteins between buthids and euscorpiids. Fifteen types of venom Peptides and Proteins were sequenced during the venom gland transcriptome analyses of two Buthidae species (Lychas mucronatus and Isometrus maculatus) and one Euscorpiidae species (Scorpiops margerisonae). Great diversity has been observed in translated amino acid sequences of these transcripts for venom Peptides and Proteins. Seven types of venom Peptides and Proteins were shared between buthids and euscorpiids. Molecular phylogenetic analysis revealed that at least five of the seven common types of venom Peptides and Proteins were likely recruited into the scorpion venom proteome before the lineage split between Buthidae and Euscorpiidae with their corresponding genes undergoing individual or multiple gene duplication events. These are α-KTxs, βKSPNs (β-KTxs and scorpines), anionic Peptides, La1-like Peptides, and SPSVs (serine proteases from scorpion venom). Multiple types of venom Peptides and Proteins were demonstrated to be continuously recruited into the venom proteome during the evolution process of individual scorpion lineages. Our results provide an insight into the recruitment pattern of the scorpion venom arsenal for the first time.
Akira Naito - One of the best experts on this subject based on the ideXlab platform.
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Structure Determination of Membrane Peptides and Proteins by Solid-State NMR
Experimental Approaches of NMR Spectroscopy, 2017Co-Authors: Izuru Kawamura, Kazushi Norisada, Akira NaitoAbstract:Solid-state nuclear magnetic resonance (NMR) spectroscopy provides useful information on the structure, topology, and orientation of Peptides and Proteins bound to lipid bilayers. The structure and orientation of membrane-associated Peptides and Proteins can be elucidated by analyzing structural constraints obtained from anisotropic chemical-shift interactions, nuclear dipolar interactions, or a combination of these interactions. Detailed structures of various Peptides and Proteins in their membrane-bound states can be studied by analyzing anisotropic chemical-shift interactions by, for example, chemical-shift oscillation analysis, and nuclear dipolar interactions using techniques such as polarity index slant angle wheel analysis. Magic-angle spinning (MAS) experiments coupled with cross-polarization (CP) and high-power decoupling (CP-MAS) techniques provide high-resolution 13C and 15N NMR signals for selectively or uniformly labeled membrane-bound Peptides and Proteins in solid-state NMR. Furthermore, homonuclear and heteronuclear dipolar interactions can be recoupled using various spin manipulation pulse sequences under MAS conditions. These experiments enable the correlation of 13C–13C and 13C–15N signals, allowing their assignment to specific amino acid residues and ultimately determination of the high-resolution structure of membrane-bound Peptides and Proteins.
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Recent Solid-State NMR Studies of Membrane-Bound Peptides and Proteins
Annual Reports on NMR Spectroscopy, 2015Co-Authors: Akira Naito, Izuru Kawamura, Namsrai JavkhlantugsAbstract:Abstract Solid-state nuclear magnetic resonance (NMR) spectroscopy provides useful information on the structure, topology, and orientation of Peptides and Proteins bound to lipid bilayers. The structure and orientation of membrane-associated Peptides and Proteins can be elucidated by analyzing structural constraints obtained from anisotropic chemical-shift interactions such as chemical-shift oscillation or nuclear dipole interactions (e.g., dipolar waves) or a combination of thereof (e.g., polarity index slant angle [PISA] wheel patterns). Detailed structural determinations of various Peptides and Proteins in the membrane-bound state are presented. Magic-angle spinning (MAS) experiments considered with cross-polarization (CP) and high-power decoupling (CP-MAS) provide high-resolution 13 C- and 15 N-NMR signals for selectively or uniformly labeled membrane-bound Peptides and Proteins. In solid-state NMR, homonuclear and heteronuclear dipolar interactions are recoupled using various spin manipulation pulse sequences under MAS conditions. These experiments enable the correlation of 13 C– 13 C and 15 N– 13 C signals for assignment to amino acid residues. These resulting data make it possible to determine the high-resolution structures of membrane-bound Peptides and Proteins. Molecular dynamics (MD) simulation is a useful tool for investigating the dynamic structures of biological molecules in membrane environments. Applications of MD simulation to membrane-bound Peptides and Proteins are also reviewed.
Namsrai Javkhlantugs - One of the best experts on this subject based on the ideXlab platform.
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Recent Solid-State NMR Studies of Membrane-Bound Peptides and Proteins
Annual Reports on NMR Spectroscopy, 2015Co-Authors: Akira Naito, Izuru Kawamura, Namsrai JavkhlantugsAbstract:Abstract Solid-state nuclear magnetic resonance (NMR) spectroscopy provides useful information on the structure, topology, and orientation of Peptides and Proteins bound to lipid bilayers. The structure and orientation of membrane-associated Peptides and Proteins can be elucidated by analyzing structural constraints obtained from anisotropic chemical-shift interactions such as chemical-shift oscillation or nuclear dipole interactions (e.g., dipolar waves) or a combination of thereof (e.g., polarity index slant angle [PISA] wheel patterns). Detailed structural determinations of various Peptides and Proteins in the membrane-bound state are presented. Magic-angle spinning (MAS) experiments considered with cross-polarization (CP) and high-power decoupling (CP-MAS) provide high-resolution 13 C- and 15 N-NMR signals for selectively or uniformly labeled membrane-bound Peptides and Proteins. In solid-state NMR, homonuclear and heteronuclear dipolar interactions are recoupled using various spin manipulation pulse sequences under MAS conditions. These experiments enable the correlation of 13 C– 13 C and 15 N– 13 C signals for assignment to amino acid residues. These resulting data make it possible to determine the high-resolution structures of membrane-bound Peptides and Proteins. Molecular dynamics (MD) simulation is a useful tool for investigating the dynamic structures of biological molecules in membrane environments. Applications of MD simulation to membrane-bound Peptides and Proteins are also reviewed.
Bernard Lebleu - One of the best experts on this subject based on the ideXlab platform.
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One-pot labeling and purification of Peptides and Proteins with fluorescein maleimide
Tetrahedron Letters, 2003Co-Authors: Eric Vivès, Bernard LebleuAbstract:Fluorescein labeling of Peptides and Proteins is required for numerous biophysical or biological experiments such as fluorescence microscopy, fluorescence resonance energy transfer (FRET) or fluorescence imaging. The commonly used strategy relied on the coupling of the dye reagent followed by a gel filtration to recover the labeled molecule. Here we report a simplified method for the labeling of Peptides and Proteins on a cysteine residue and their purification. The method is based on the precipitation of Peptides and Proteins in acetone, fluorescein maleimide being soluble in this solvent. The excess of dye is fully eliminated after a couple of acetone washes and the precipitated peptide or protein is readily recovered.
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One-pot labeling and purification of Peptides and Proteins with fluorescein maleimide
Tetrahedron Letters, 2003Co-Authors: Eric Vivès, Bernard LebleuAbstract:Fluorescein labeling of Peptides and Proteins is required for numerous biophysical or biological experiments such as fluorescence microscopy, fluorescence resonance energy transfer (FRET) or fluorescence imaging. The commonly used strategy relied on the coupling of the dye reagent followed by a gel filtration to recover the labeled molecule. Here we report a simplified method for the labeling of Peptides and Proteins on a cysteine residue and their purification. The method is based on the precipitation of Peptides and Proteins in acetone, fluorescein maleimide being soluble in this solvent. The excess of dye is fully eliminated after a couple of acetone washes and the precipitated peptide or protein is readily recovered. (C) 2003 Elsevier Science Ltd. All rights reserved.
Ruiming Zhao - One of the best experts on this subject based on the ideXlab platform.
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Extreme diversity of scorpion venom Peptides and Proteins revealed by transcriptomic analysis: Implication for proteome evolution of scorpion venom arsenal
Journal of Proteomics, 2012Co-Authors: Ruiming Zhao, Zhijian CaoAbstract:Venom is an important genetic development crucial to the survival of scorpions for over 400 million years. We studied the evolution of the scorpion venom arsenal by means of comparative transcriptome analysis of venom glands and phylogenetic analysis of shared types of venom Peptides and Proteins between buthids and euscorpiids. Fifteen types of venom Peptides and Proteins were sequenced during the venom gland transcriptome analyses of two Buthidae species (Lychas mucronatus and Isometrus maculatus) and one Euscorpiidae species (Scorpiops margerisonae). Great diversity has been observed in translated amino acid sequences of these transcripts for venom Peptides and Proteins. Seven types of venom Peptides and Proteins were shared between buthids and euscorpiids. Molecular phylogenetic analysis revealed that at least five of the seven common types of venom Peptides and Proteins were likely recruited into the scorpion venom proteome before the lineage split between Buthidae and Euscorpiidae with their corresponding genes undergoing individual or multiple gene duplication events. These are α-KTxs, βKSPNs (β-KTxs and scorpines), anionic Peptides, La1-like Peptides, and SPSVs (serine proteases from scorpion venom). Multiple types of venom Peptides and Proteins were demonstrated to be continuously recruited into the venom proteome during the evolution process of individual scorpion lineages. Our results provide an insight into the recruitment pattern of the scorpion venom arsenal for the first time.