The Experts below are selected from a list of 3669 Experts worldwide ranked by ideXlab platform
Yuzhu Zhang - One of the best experts on this subject based on the ideXlab platform.
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Isolation and characterization of Korean Pine (Pinus koraiensis) convicilin.
Plant physiology and biochemistry : PPB, 2014Co-Authors: Tengchuan Jin, Yang Wang, Yu-wei Chen, Silvia M. Albillos, Mahendra H. Kothary, Boyce Tankersley, Tara H. Mchugh, Yuzhu ZhangAbstract:A vicilin-like globulin seed storage protein, termed convicilin, was isolated for the first time from Korean Pine (Pinus koraiensis). SDS-PAGE analysis revealed that Korean Pine convicilin was post-translationally processed. The N-terminal peptide sequences of its components were determined. These peptides could be mapped to a protein translated from an embryo abundant transcript isolated in this study. Similar to vicilin, native convicilin appeared to be homotrimeric. Differential scanning calorimetry (DSC) analyses revealed that this protein is less resistant to thermal treatment than Korean Pine vicilin. Its transition temperature was 75.57 °C compared with 84.13 °C for vicilin. The urea induced folding-unfolding equilibrium of Pine convicilin monitored by intrinsic fluorescence could be interpreted in terms of a two-state model, with a Cm of 4.41 ± 0.15 M.
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crystal structure of Korean Pine pinus koraiensis 7s seed storage protein with copper ligands
Journal of Agricultural and Food Chemistry, 2014Co-Authors: Yang Wang, Yu-wei Chen, Mahendra H. Kothary, Tara H. Mchugh, Tongjen Fu, Yuzhu ZhangAbstract:The prevalence of food allergy has increased in recent years, and Korean Pine vicilin is a potential food allergen. We have previously reported the crystallization of Korean Pine vicilin purified from raw Pine nut. Here we report the isolation of vicilin mRNA and the crystal structure of Korean Pine vicilin at 2.40 A resolution. The overall structure of Pine nut vicilin is similar to the structures of other 7S seed storage proteins and consists of an N-terminal domain and a C-terminal domain. Each assumes a cupin fold, and they are symmetrically related about a pseudodyad axis. Three vicilin molecules form a doughnut-shaped trimer through head-to-tail association. Structure characterization of Korean Pine nut vicilin unexpectedly showed that, in its native trimeric state, the vicilin has three copper ligands. Sequence alignments suggested that the copper-coordinating residues were conserved in winter squash, sesame, tomato, and several tree nuts, while they were not conserved in a number of legumes, inclu...
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Crystal Structure of Korean Pine (Pinus koraiensis) 7S Seed Storage Protein with Copper Ligands
Journal of agricultural and food chemistry, 2013Co-Authors: Tengchuan Jin, Yang Wang, Yu-wei Chen, Mahendra H. Kothary, Tara H. Mchugh, Yuzhu ZhangAbstract:The prevalence of food allergy has increased in recent years, and Korean Pine vicilin is a potential food allergen. We have previously reported the crystallization of Korean Pine vicilin purified f...
Yang Wang - One of the best experts on this subject based on the ideXlab platform.
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Isolation and characterization of Korean Pine (Pinus koraiensis) convicilin.
Plant physiology and biochemistry : PPB, 2014Co-Authors: Tengchuan Jin, Yang Wang, Yu-wei Chen, Silvia M. Albillos, Mahendra H. Kothary, Boyce Tankersley, Tara H. Mchugh, Yuzhu ZhangAbstract:A vicilin-like globulin seed storage protein, termed convicilin, was isolated for the first time from Korean Pine (Pinus koraiensis). SDS-PAGE analysis revealed that Korean Pine convicilin was post-translationally processed. The N-terminal peptide sequences of its components were determined. These peptides could be mapped to a protein translated from an embryo abundant transcript isolated in this study. Similar to vicilin, native convicilin appeared to be homotrimeric. Differential scanning calorimetry (DSC) analyses revealed that this protein is less resistant to thermal treatment than Korean Pine vicilin. Its transition temperature was 75.57 °C compared with 84.13 °C for vicilin. The urea induced folding-unfolding equilibrium of Pine convicilin monitored by intrinsic fluorescence could be interpreted in terms of a two-state model, with a Cm of 4.41 ± 0.15 M.
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crystal structure of Korean Pine pinus koraiensis 7s seed storage protein with copper ligands
Journal of Agricultural and Food Chemistry, 2014Co-Authors: Yang Wang, Yu-wei Chen, Mahendra H. Kothary, Tara H. Mchugh, Tongjen Fu, Yuzhu ZhangAbstract:The prevalence of food allergy has increased in recent years, and Korean Pine vicilin is a potential food allergen. We have previously reported the crystallization of Korean Pine vicilin purified from raw Pine nut. Here we report the isolation of vicilin mRNA and the crystal structure of Korean Pine vicilin at 2.40 A resolution. The overall structure of Pine nut vicilin is similar to the structures of other 7S seed storage proteins and consists of an N-terminal domain and a C-terminal domain. Each assumes a cupin fold, and they are symmetrically related about a pseudodyad axis. Three vicilin molecules form a doughnut-shaped trimer through head-to-tail association. Structure characterization of Korean Pine nut vicilin unexpectedly showed that, in its native trimeric state, the vicilin has three copper ligands. Sequence alignments suggested that the copper-coordinating residues were conserved in winter squash, sesame, tomato, and several tree nuts, while they were not conserved in a number of legumes, inclu...
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Crystal Structure of Korean Pine (Pinus koraiensis) 7S Seed Storage Protein with Copper Ligands
Journal of agricultural and food chemistry, 2013Co-Authors: Tengchuan Jin, Yang Wang, Yu-wei Chen, Mahendra H. Kothary, Tara H. Mchugh, Yuzhu ZhangAbstract:The prevalence of food allergy has increased in recent years, and Korean Pine vicilin is a potential food allergen. We have previously reported the crystallization of Korean Pine vicilin purified f...
Mahendra H. Kothary - One of the best experts on this subject based on the ideXlab platform.
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Isolation and characterization of Korean Pine (Pinus koraiensis) convicilin.
Plant physiology and biochemistry : PPB, 2014Co-Authors: Tengchuan Jin, Yang Wang, Yu-wei Chen, Silvia M. Albillos, Mahendra H. Kothary, Boyce Tankersley, Tara H. Mchugh, Yuzhu ZhangAbstract:A vicilin-like globulin seed storage protein, termed convicilin, was isolated for the first time from Korean Pine (Pinus koraiensis). SDS-PAGE analysis revealed that Korean Pine convicilin was post-translationally processed. The N-terminal peptide sequences of its components were determined. These peptides could be mapped to a protein translated from an embryo abundant transcript isolated in this study. Similar to vicilin, native convicilin appeared to be homotrimeric. Differential scanning calorimetry (DSC) analyses revealed that this protein is less resistant to thermal treatment than Korean Pine vicilin. Its transition temperature was 75.57 °C compared with 84.13 °C for vicilin. The urea induced folding-unfolding equilibrium of Pine convicilin monitored by intrinsic fluorescence could be interpreted in terms of a two-state model, with a Cm of 4.41 ± 0.15 M.
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crystal structure of Korean Pine pinus koraiensis 7s seed storage protein with copper ligands
Journal of Agricultural and Food Chemistry, 2014Co-Authors: Yang Wang, Yu-wei Chen, Mahendra H. Kothary, Tara H. Mchugh, Tongjen Fu, Yuzhu ZhangAbstract:The prevalence of food allergy has increased in recent years, and Korean Pine vicilin is a potential food allergen. We have previously reported the crystallization of Korean Pine vicilin purified from raw Pine nut. Here we report the isolation of vicilin mRNA and the crystal structure of Korean Pine vicilin at 2.40 A resolution. The overall structure of Pine nut vicilin is similar to the structures of other 7S seed storage proteins and consists of an N-terminal domain and a C-terminal domain. Each assumes a cupin fold, and they are symmetrically related about a pseudodyad axis. Three vicilin molecules form a doughnut-shaped trimer through head-to-tail association. Structure characterization of Korean Pine nut vicilin unexpectedly showed that, in its native trimeric state, the vicilin has three copper ligands. Sequence alignments suggested that the copper-coordinating residues were conserved in winter squash, sesame, tomato, and several tree nuts, while they were not conserved in a number of legumes, inclu...
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Crystal Structure of Korean Pine (Pinus koraiensis) 7S Seed Storage Protein with Copper Ligands
Journal of agricultural and food chemistry, 2013Co-Authors: Tengchuan Jin, Yang Wang, Yu-wei Chen, Mahendra H. Kothary, Tara H. Mchugh, Yuzhu ZhangAbstract:The prevalence of food allergy has increased in recent years, and Korean Pine vicilin is a potential food allergen. We have previously reported the crystallization of Korean Pine vicilin purified f...
Tara H. Mchugh - One of the best experts on this subject based on the ideXlab platform.
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Isolation and characterization of Korean Pine (Pinus koraiensis) convicilin.
Plant physiology and biochemistry : PPB, 2014Co-Authors: Tengchuan Jin, Yang Wang, Yu-wei Chen, Silvia M. Albillos, Mahendra H. Kothary, Boyce Tankersley, Tara H. Mchugh, Yuzhu ZhangAbstract:A vicilin-like globulin seed storage protein, termed convicilin, was isolated for the first time from Korean Pine (Pinus koraiensis). SDS-PAGE analysis revealed that Korean Pine convicilin was post-translationally processed. The N-terminal peptide sequences of its components were determined. These peptides could be mapped to a protein translated from an embryo abundant transcript isolated in this study. Similar to vicilin, native convicilin appeared to be homotrimeric. Differential scanning calorimetry (DSC) analyses revealed that this protein is less resistant to thermal treatment than Korean Pine vicilin. Its transition temperature was 75.57 °C compared with 84.13 °C for vicilin. The urea induced folding-unfolding equilibrium of Pine convicilin monitored by intrinsic fluorescence could be interpreted in terms of a two-state model, with a Cm of 4.41 ± 0.15 M.
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crystal structure of Korean Pine pinus koraiensis 7s seed storage protein with copper ligands
Journal of Agricultural and Food Chemistry, 2014Co-Authors: Yang Wang, Yu-wei Chen, Mahendra H. Kothary, Tara H. Mchugh, Tongjen Fu, Yuzhu ZhangAbstract:The prevalence of food allergy has increased in recent years, and Korean Pine vicilin is a potential food allergen. We have previously reported the crystallization of Korean Pine vicilin purified from raw Pine nut. Here we report the isolation of vicilin mRNA and the crystal structure of Korean Pine vicilin at 2.40 A resolution. The overall structure of Pine nut vicilin is similar to the structures of other 7S seed storage proteins and consists of an N-terminal domain and a C-terminal domain. Each assumes a cupin fold, and they are symmetrically related about a pseudodyad axis. Three vicilin molecules form a doughnut-shaped trimer through head-to-tail association. Structure characterization of Korean Pine nut vicilin unexpectedly showed that, in its native trimeric state, the vicilin has three copper ligands. Sequence alignments suggested that the copper-coordinating residues were conserved in winter squash, sesame, tomato, and several tree nuts, while they were not conserved in a number of legumes, inclu...
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Crystal Structure of Korean Pine (Pinus koraiensis) 7S Seed Storage Protein with Copper Ligands
Journal of agricultural and food chemistry, 2013Co-Authors: Tengchuan Jin, Yang Wang, Yu-wei Chen, Mahendra H. Kothary, Tara H. Mchugh, Yuzhu ZhangAbstract:The prevalence of food allergy has increased in recent years, and Korean Pine vicilin is a potential food allergen. We have previously reported the crystallization of Korean Pine vicilin purified f...
Yu-wei Chen - One of the best experts on this subject based on the ideXlab platform.
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Isolation and characterization of Korean Pine (Pinus koraiensis) convicilin.
Plant physiology and biochemistry : PPB, 2014Co-Authors: Tengchuan Jin, Yang Wang, Yu-wei Chen, Silvia M. Albillos, Mahendra H. Kothary, Boyce Tankersley, Tara H. Mchugh, Yuzhu ZhangAbstract:A vicilin-like globulin seed storage protein, termed convicilin, was isolated for the first time from Korean Pine (Pinus koraiensis). SDS-PAGE analysis revealed that Korean Pine convicilin was post-translationally processed. The N-terminal peptide sequences of its components were determined. These peptides could be mapped to a protein translated from an embryo abundant transcript isolated in this study. Similar to vicilin, native convicilin appeared to be homotrimeric. Differential scanning calorimetry (DSC) analyses revealed that this protein is less resistant to thermal treatment than Korean Pine vicilin. Its transition temperature was 75.57 °C compared with 84.13 °C for vicilin. The urea induced folding-unfolding equilibrium of Pine convicilin monitored by intrinsic fluorescence could be interpreted in terms of a two-state model, with a Cm of 4.41 ± 0.15 M.
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crystal structure of Korean Pine pinus koraiensis 7s seed storage protein with copper ligands
Journal of Agricultural and Food Chemistry, 2014Co-Authors: Yang Wang, Yu-wei Chen, Mahendra H. Kothary, Tara H. Mchugh, Tongjen Fu, Yuzhu ZhangAbstract:The prevalence of food allergy has increased in recent years, and Korean Pine vicilin is a potential food allergen. We have previously reported the crystallization of Korean Pine vicilin purified from raw Pine nut. Here we report the isolation of vicilin mRNA and the crystal structure of Korean Pine vicilin at 2.40 A resolution. The overall structure of Pine nut vicilin is similar to the structures of other 7S seed storage proteins and consists of an N-terminal domain and a C-terminal domain. Each assumes a cupin fold, and they are symmetrically related about a pseudodyad axis. Three vicilin molecules form a doughnut-shaped trimer through head-to-tail association. Structure characterization of Korean Pine nut vicilin unexpectedly showed that, in its native trimeric state, the vicilin has three copper ligands. Sequence alignments suggested that the copper-coordinating residues were conserved in winter squash, sesame, tomato, and several tree nuts, while they were not conserved in a number of legumes, inclu...
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Crystal Structure of Korean Pine (Pinus koraiensis) 7S Seed Storage Protein with Copper Ligands
Journal of agricultural and food chemistry, 2013Co-Authors: Tengchuan Jin, Yang Wang, Yu-wei Chen, Mahendra H. Kothary, Tara H. Mchugh, Yuzhu ZhangAbstract:The prevalence of food allergy has increased in recent years, and Korean Pine vicilin is a potential food allergen. We have previously reported the crystallization of Korean Pine vicilin purified f...
