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Ahmed Al-harrasi - One of the best experts on this subject based on the ideXlab platform.
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The molecular mass and Isoelectric Point of plant proteomes
BMC Genomics, 2019Co-Authors: Tapan Kumar Mohanta, Abdullatif Khan, Abeer Hashem, Elsayed Fathi Abd_allah, Ahmed Al-harrasiAbstract:Background Cell contain diverse array of proteins with different molecular weight and Isoelectric Point (pI). The molecular weight and pI of protein play important role in determining the molecular biochemical function. Therefore, it was important to understand the detail regarding the molecular weight and pI of the plant proteins. Results A proteome-wide analysis of plant proteomes from 145 species revealed a pI range of 1.99 (epsin) to 13.96 (hypothetical protein). The spectrum of molecular mass of the plant proteins varied from 0.54 to 2236.8 kDa. A putative Type-I polyketide synthase (22244 amino acids) in Volvox carteri was found to be the largest protein in the plant kingdom. However, Type-I polyketide synthase was not found in higher plant species. Titin (806.46 kDa) and misin/midasin (730.02 kDa) were the largest proteins identified in higher plant species. The pI and molecular weight of the plant proteins showed a trimodal distribution. An acidic pI (56.44% of proteins) was found to be predominant over a basic pI (43.34% of proteins) and the abundance of acidic pI proteins was higher in unicellular algae species relative to multicellular higher plants. In contrast, the seaweed, Porphyra umbilicalis , possesses a higher proportion of basic pI proteins (70.09%). Plant proteomes were also found to contain selenocysteine (Sec), amino acid that was found only in lower eukaryotic aquatic plant lineage. Amino acid composition analysis showed Leu was high and Trp was low abundant amino acids in the plant proteome. Additionally, the plant proteomes also possess ambiguous amino acids Xaa (unknown), Asx (asparagine or aspartic acid), Glx (glutamine or glutamic acid), and Xle (leucine or isoleucine) as well. Conclusion The diverse molecular weight and Isoelectric Point range of plant proteome will be helpful to understand their biochemical and functional aspects. The presence of selenocysteine proteins in lower eukaryotic organism is of interest and their expression in higher plant system can help us to understand their functional role.
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The molecular mass and Isoelectric Point of plant proteomes
BMC genomics, 2019Co-Authors: Tapan Kumar Mohanta, Abdullatif Khan, Abeer Hashem, Elsayed Fathi Abd_allah, Ahmed Al-harrasiAbstract:Cell contain diverse array of proteins with different molecular weight and Isoelectric Point (pI). The molecular weight and pI of protein play important role in determining the molecular biochemical function. Therefore, it was important to understand the detail regarding the molecular weight and pI of the plant proteins. A proteome-wide analysis of plant proteomes from 145 species revealed a pI range of 1.99 (epsin) to 13.96 (hypothetical protein). The spectrum of molecular mass of the plant proteins varied from 0.54 to 2236.8 kDa. A putative Type-I polyketide synthase (22244 amino acids) in Volvox carteri was found to be the largest protein in the plant kingdom. However, Type-I polyketide synthase was not found in higher plant species. Titin (806.46 kDa) and misin/midasin (730.02 kDa) were the largest proteins identified in higher plant species. The pI and molecular weight of the plant proteins showed a trimodal distribution. An acidic pI (56.44% of proteins) was found to be predominant over a basic pI (43.34% of proteins) and the abundance of acidic pI proteins was higher in unicellular algae species relative to multicellular higher plants. In contrast, the seaweed, Porphyra umbilicalis, possesses a higher proportion of basic pI proteins (70.09%). Plant proteomes were also found to contain selenocysteine (Sec), amino acid that was found only in lower eukaryotic aquatic plant lineage. Amino acid composition analysis showed Leu was high and Trp was low abundant amino acids in the plant proteome. Additionally, the plant proteomes also possess ambiguous amino acids Xaa (unknown), Asx (asparagine or aspartic acid), Glx (glutamine or glutamic acid), and Xle (leucine or isoleucine) as well. The diverse molecular weight and Isoelectric Point range of plant proteome will be helpful to understand their biochemical and functional aspects. The presence of selenocysteine proteins in lower eukaryotic organism is of interest and their expression in higher plant system can help us to understand their functional role.
Keith L Williams - One of the best experts on this subject based on the ideXlab platform.
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cross species protein identification using amino acid composition peptide mass fingerprinting Isoelectric Point and molecular mass a theoretical evaluation
Journal of Theoretical Biology, 1997Co-Authors: Marc R Wilkins, Keith L WilliamsAbstract:Abstract Proteins can be identified by rapid techniques that do not involve Edman degradation sequencing. These approaches entail the matching of amino acid compositions or tryptic peptide masses of proteins against databases, often in conjunction with estimated protein molecular weight and Isoelectric Point. As genome sequencing projects progress, proteins from poorly molecularly defined organisms will increasingly be identified by cross-species comparison to proteins from well-defined organisms. To investigate the application of rapid techniques for cross-species protein identification, a total of 65 theoretical cross-species comparisons involving 21 proteins (nine human and 12 E. coli ) were undertaken. The degree of conservation of amino acid composition, tryptic peptides, protein Isoelectric Point and mass was established. Protein amino acid composition was well conserved across species boundaries, whilst tryptic peptides were poorly conserved. The molecular weight of proteins was generally well conserved, but protein Isoelectric Point was not. These results suggest that cross-species protein identification by rapid techniques will be done by protein amino acid composition and protein molecular weight.
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cross species protein identification using amino acid composition peptide mass fingerprinting Isoelectric Point and molecular mass a theoretical evaluation
Journal of Theoretical Biology, 1997Co-Authors: Marc R Wilkins, Keith L WilliamsAbstract:Proteins can be identified by rapid techniques that do not involve Edman degradation sequencing. These approaches entail the matching of amino acid compositions or tryptic peptide masses of proteins against databases, often in conjunction with estimated protein molecular weight and Isoelectric Point. As genome sequencing projects progress, proteins from poorly molecularly defined organisms will increasingly be identified by cross-species comparison to proteins from well-defined organisms. To investigate the application of rapid techniques for cross-species protein identification, a total of 65 theoretical cross-species comparisons involving 21 proteins (nine human and 12 E. coli) were undertaken. The degree of conservation of amino acid composition, tryptic peptides, protein Isoelectric Point and mass was established. Protein amino acid composition was well conserved across species boundaries, whilst tryptic peptides were poorly conserved. The molecular weight of proteins was generally well conserved, but protein Isoelectric Point was not. These results suggest that cross-species protein identification by rapid techniques will be done best by protein amino acid composition and protein molecular weight.
Tapan Kumar Mohanta - One of the best experts on this subject based on the ideXlab platform.
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The molecular mass and Isoelectric Point of plant proteomes
BMC Genomics, 2019Co-Authors: Tapan Kumar Mohanta, Abdullatif Khan, Abeer Hashem, Elsayed Fathi Abd_allah, Ahmed Al-harrasiAbstract:Background Cell contain diverse array of proteins with different molecular weight and Isoelectric Point (pI). The molecular weight and pI of protein play important role in determining the molecular biochemical function. Therefore, it was important to understand the detail regarding the molecular weight and pI of the plant proteins. Results A proteome-wide analysis of plant proteomes from 145 species revealed a pI range of 1.99 (epsin) to 13.96 (hypothetical protein). The spectrum of molecular mass of the plant proteins varied from 0.54 to 2236.8 kDa. A putative Type-I polyketide synthase (22244 amino acids) in Volvox carteri was found to be the largest protein in the plant kingdom. However, Type-I polyketide synthase was not found in higher plant species. Titin (806.46 kDa) and misin/midasin (730.02 kDa) were the largest proteins identified in higher plant species. The pI and molecular weight of the plant proteins showed a trimodal distribution. An acidic pI (56.44% of proteins) was found to be predominant over a basic pI (43.34% of proteins) and the abundance of acidic pI proteins was higher in unicellular algae species relative to multicellular higher plants. In contrast, the seaweed, Porphyra umbilicalis , possesses a higher proportion of basic pI proteins (70.09%). Plant proteomes were also found to contain selenocysteine (Sec), amino acid that was found only in lower eukaryotic aquatic plant lineage. Amino acid composition analysis showed Leu was high and Trp was low abundant amino acids in the plant proteome. Additionally, the plant proteomes also possess ambiguous amino acids Xaa (unknown), Asx (asparagine or aspartic acid), Glx (glutamine or glutamic acid), and Xle (leucine or isoleucine) as well. Conclusion The diverse molecular weight and Isoelectric Point range of plant proteome will be helpful to understand their biochemical and functional aspects. The presence of selenocysteine proteins in lower eukaryotic organism is of interest and their expression in higher plant system can help us to understand their functional role.
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The molecular mass and Isoelectric Point of plant proteomes
BMC genomics, 2019Co-Authors: Tapan Kumar Mohanta, Abdullatif Khan, Abeer Hashem, Elsayed Fathi Abd_allah, Ahmed Al-harrasiAbstract:Cell contain diverse array of proteins with different molecular weight and Isoelectric Point (pI). The molecular weight and pI of protein play important role in determining the molecular biochemical function. Therefore, it was important to understand the detail regarding the molecular weight and pI of the plant proteins. A proteome-wide analysis of plant proteomes from 145 species revealed a pI range of 1.99 (epsin) to 13.96 (hypothetical protein). The spectrum of molecular mass of the plant proteins varied from 0.54 to 2236.8 kDa. A putative Type-I polyketide synthase (22244 amino acids) in Volvox carteri was found to be the largest protein in the plant kingdom. However, Type-I polyketide synthase was not found in higher plant species. Titin (806.46 kDa) and misin/midasin (730.02 kDa) were the largest proteins identified in higher plant species. The pI and molecular weight of the plant proteins showed a trimodal distribution. An acidic pI (56.44% of proteins) was found to be predominant over a basic pI (43.34% of proteins) and the abundance of acidic pI proteins was higher in unicellular algae species relative to multicellular higher plants. In contrast, the seaweed, Porphyra umbilicalis, possesses a higher proportion of basic pI proteins (70.09%). Plant proteomes were also found to contain selenocysteine (Sec), amino acid that was found only in lower eukaryotic aquatic plant lineage. Amino acid composition analysis showed Leu was high and Trp was low abundant amino acids in the plant proteome. Additionally, the plant proteomes also possess ambiguous amino acids Xaa (unknown), Asx (asparagine or aspartic acid), Glx (glutamine or glutamic acid), and Xle (leucine or isoleucine) as well. The diverse molecular weight and Isoelectric Point range of plant proteome will be helpful to understand their biochemical and functional aspects. The presence of selenocysteine proteins in lower eukaryotic organism is of interest and their expression in higher plant system can help us to understand their functional role.
Harry Boer - One of the best experts on this subject based on the ideXlab platform.
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Sodium caseinates with an altered Isoelectric Point as emulsifiers in oil/water systems.
Journal of agricultural and food chemistry, 2009Co-Authors: Pirkko Forssell, Riitta Partanen, Rauni Seppänen, Johanna Buchert, Harry BoerAbstract:Sodium caseinate was chemically modified in order to alter its Isoelectric Point (pI). Negatively charged carboxylic groups were introduced to lower the pI, and positively charged amino groups to a...
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sodium caseinates with an altered Isoelectric Point as emulsifiers in oil water systems
Journal of Agricultural and Food Chemistry, 2009Co-Authors: Pirkko Forssell, Riitta Partanen, Rauni Seppänen, Johanna Buchert, Harry BoerAbstract:Sodium caseinate was chemically modified in order to alter its Isoelectric Point (pI). Negatively charged carboxylic groups were introduced to lower the pI, and positively charged amino groups to a...
Abdullatif Khan - One of the best experts on this subject based on the ideXlab platform.
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The molecular mass and Isoelectric Point of plant proteomes
BMC Genomics, 2019Co-Authors: Tapan Kumar Mohanta, Abdullatif Khan, Abeer Hashem, Elsayed Fathi Abd_allah, Ahmed Al-harrasiAbstract:Background Cell contain diverse array of proteins with different molecular weight and Isoelectric Point (pI). The molecular weight and pI of protein play important role in determining the molecular biochemical function. Therefore, it was important to understand the detail regarding the molecular weight and pI of the plant proteins. Results A proteome-wide analysis of plant proteomes from 145 species revealed a pI range of 1.99 (epsin) to 13.96 (hypothetical protein). The spectrum of molecular mass of the plant proteins varied from 0.54 to 2236.8 kDa. A putative Type-I polyketide synthase (22244 amino acids) in Volvox carteri was found to be the largest protein in the plant kingdom. However, Type-I polyketide synthase was not found in higher plant species. Titin (806.46 kDa) and misin/midasin (730.02 kDa) were the largest proteins identified in higher plant species. The pI and molecular weight of the plant proteins showed a trimodal distribution. An acidic pI (56.44% of proteins) was found to be predominant over a basic pI (43.34% of proteins) and the abundance of acidic pI proteins was higher in unicellular algae species relative to multicellular higher plants. In contrast, the seaweed, Porphyra umbilicalis , possesses a higher proportion of basic pI proteins (70.09%). Plant proteomes were also found to contain selenocysteine (Sec), amino acid that was found only in lower eukaryotic aquatic plant lineage. Amino acid composition analysis showed Leu was high and Trp was low abundant amino acids in the plant proteome. Additionally, the plant proteomes also possess ambiguous amino acids Xaa (unknown), Asx (asparagine or aspartic acid), Glx (glutamine or glutamic acid), and Xle (leucine or isoleucine) as well. Conclusion The diverse molecular weight and Isoelectric Point range of plant proteome will be helpful to understand their biochemical and functional aspects. The presence of selenocysteine proteins in lower eukaryotic organism is of interest and their expression in higher plant system can help us to understand their functional role.
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The molecular mass and Isoelectric Point of plant proteomes
BMC genomics, 2019Co-Authors: Tapan Kumar Mohanta, Abdullatif Khan, Abeer Hashem, Elsayed Fathi Abd_allah, Ahmed Al-harrasiAbstract:Cell contain diverse array of proteins with different molecular weight and Isoelectric Point (pI). The molecular weight and pI of protein play important role in determining the molecular biochemical function. Therefore, it was important to understand the detail regarding the molecular weight and pI of the plant proteins. A proteome-wide analysis of plant proteomes from 145 species revealed a pI range of 1.99 (epsin) to 13.96 (hypothetical protein). The spectrum of molecular mass of the plant proteins varied from 0.54 to 2236.8 kDa. A putative Type-I polyketide synthase (22244 amino acids) in Volvox carteri was found to be the largest protein in the plant kingdom. However, Type-I polyketide synthase was not found in higher plant species. Titin (806.46 kDa) and misin/midasin (730.02 kDa) were the largest proteins identified in higher plant species. The pI and molecular weight of the plant proteins showed a trimodal distribution. An acidic pI (56.44% of proteins) was found to be predominant over a basic pI (43.34% of proteins) and the abundance of acidic pI proteins was higher in unicellular algae species relative to multicellular higher plants. In contrast, the seaweed, Porphyra umbilicalis, possesses a higher proportion of basic pI proteins (70.09%). Plant proteomes were also found to contain selenocysteine (Sec), amino acid that was found only in lower eukaryotic aquatic plant lineage. Amino acid composition analysis showed Leu was high and Trp was low abundant amino acids in the plant proteome. Additionally, the plant proteomes also possess ambiguous amino acids Xaa (unknown), Asx (asparagine or aspartic acid), Glx (glutamine or glutamic acid), and Xle (leucine or isoleucine) as well. The diverse molecular weight and Isoelectric Point range of plant proteome will be helpful to understand their biochemical and functional aspects. The presence of selenocysteine proteins in lower eukaryotic organism is of interest and their expression in higher plant system can help us to understand their functional role.
