Review



protein secondary structure prediction web online tools  (Softberry Inc)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 90
      Buy from Supplier

    Structured Review

    Softberry Inc protein secondary structure prediction web online tools
    The detailed genes information of ClPRXs.
    Protein Secondary Structure Prediction Web Online Tools, supplied by Softberry Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/protein+secondary+structure+prediction+web+online+tools/protein+localization+prediction+tool/pmc08775647-303-10-17
    Average 90 stars, based on 1 article reviews
    protein secondary structure prediction web online tools - by Bioz Stars, 2026-09
    90/100 stars

    Images

    1) Product Images from "Genome-Wide Analysis of the Peroxidase Gene Family and Verification of Lignin Synthesis-Related Genes in Watermelon"

    Article Title: Genome-Wide Analysis of the Peroxidase Gene Family and Verification of Lignin Synthesis-Related Genes in Watermelon

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms23020642

    The detailed genes information of ClPRXs.
    Figure Legend Snippet: The detailed genes information of ClPRXs.

    Techniques Used: Molecular Weight

    Structural characteristics of ClPRX protein. ( A ) Schematic diagram of the primary structure of the class III peroxidase. The green boxes at the front and back signify the N-terminal signal peptide (SP) and c-terminal extension domain (CT). The middle three boxes represent the highly conserved domain: box I is the distal-heme-binding site domain; box Ⅱ is the unknown functional domain; box Ⅲ is the proximal-heme-binding site domain. The gray area with obvious variation was assumed to be a variable domain responsible for the specific catalytic function of peroxidase. The highly conserved distal histidine (Hd) and proximal histidine (HP) are heme-binding sites represented by green bars. Eight cysteines (C1–C8) are key amino acids that form disulfide bonds to form the secondary structure of peroxidase, which are represented by yellow solid circles. The four conserved disulfide bonds formed are shown as black lines in plane. ( B ) represents the four conserved domains and site location information of the third type of peroxidase, which are marked on the amino acid sequence with four different colors, and the 3D model of the structure of the four domains is displayed, the yellow part being the functional site. ( C ) is the comparison results of 7 groups of ClPRX protein sequences.
    Figure Legend Snippet: Structural characteristics of ClPRX protein. ( A ) Schematic diagram of the primary structure of the class III peroxidase. The green boxes at the front and back signify the N-terminal signal peptide (SP) and c-terminal extension domain (CT). The middle three boxes represent the highly conserved domain: box I is the distal-heme-binding site domain; box Ⅱ is the unknown functional domain; box Ⅲ is the proximal-heme-binding site domain. The gray area with obvious variation was assumed to be a variable domain responsible for the specific catalytic function of peroxidase. The highly conserved distal histidine (Hd) and proximal histidine (HP) are heme-binding sites represented by green bars. Eight cysteines (C1–C8) are key amino acids that form disulfide bonds to form the secondary structure of peroxidase, which are represented by yellow solid circles. The four conserved disulfide bonds formed are shown as black lines in plane. ( B ) represents the four conserved domains and site location information of the third type of peroxidase, which are marked on the amino acid sequence with four different colors, and the 3D model of the structure of the four domains is displayed, the yellow part being the functional site. ( C ) is the comparison results of 7 groups of ClPRX protein sequences.

    Techniques Used: Binding Assay, Functional Assay, Sequencing, Comparison

    Related Articles

    Molecular Weight:

    Article Title: Genome-Wide Analysis of the Peroxidase Gene Family and Verification of Lignin Synthesis-Related Genes in Watermelon
    Article Snippet: Online information at http://h-s.p-443.npsa-prabi.ibcp.fr.neau.vpn358.com/cgi-bin/npsa_automat.pl?page=/NPSA/npsa_gor4.html (accessed on 2 April 2021) for protein secondary structure prediction was retrieved using softberry web online tools ( http://linux1.softberry.com/berryPHTML?Topic=protcomppl&group=programs&group=Proloc (accessed on 2 April 2021)) and finally used to predict the subcellular localization of 79 ClPRX proteins.

    Binding Assay:

    Article Title: Genome-Wide Analysis of the Peroxidase Gene Family and Verification of Lignin Synthesis-Related Genes in Watermelon
    Article Snippet: Online information at http://h-s.p-443.npsa-prabi.ibcp.fr.neau.vpn358.com/cgi-bin/npsa_automat.pl?page=/NPSA/npsa_gor4.html (accessed on 2 April 2021) for protein secondary structure prediction was retrieved using softberry web online tools ( http://linux1.softberry.com/berryPHTML?Topic=protcomppl&group=programs&group=Proloc (accessed on 2 April 2021)) and finally used to predict the subcellular localization of 79 ClPRX proteins.

    Functional Assay:

    Article Title: Genome-Wide Analysis of the Peroxidase Gene Family and Verification of Lignin Synthesis-Related Genes in Watermelon
    Article Snippet: Online information at http://h-s.p-443.npsa-prabi.ibcp.fr.neau.vpn358.com/cgi-bin/npsa_automat.pl?page=/NPSA/npsa_gor4.html (accessed on 2 April 2021) for protein secondary structure prediction was retrieved using softberry web online tools ( http://linux1.softberry.com/berryPHTML?Topic=protcomppl&group=programs&group=Proloc (accessed on 2 April 2021)) and finally used to predict the subcellular localization of 79 ClPRX proteins.

    Sequencing:

    Article Title: Genome-Wide Analysis of the Peroxidase Gene Family and Verification of Lignin Synthesis-Related Genes in Watermelon
    Article Snippet: Online information at http://h-s.p-443.npsa-prabi.ibcp.fr.neau.vpn358.com/cgi-bin/npsa_automat.pl?page=/NPSA/npsa_gor4.html (accessed on 2 April 2021) for protein secondary structure prediction was retrieved using softberry web online tools ( http://linux1.softberry.com/berryPHTML?Topic=protcomppl&group=programs&group=Proloc (accessed on 2 April 2021)) and finally used to predict the subcellular localization of 79 ClPRX proteins.

    Comparison:

    Article Title: Genome-Wide Analysis of the Peroxidase Gene Family and Verification of Lignin Synthesis-Related Genes in Watermelon
    Article Snippet: Online information at http://h-s.p-443.npsa-prabi.ibcp.fr.neau.vpn358.com/cgi-bin/npsa_automat.pl?page=/NPSA/npsa_gor4.html (accessed on 2 April 2021) for protein secondary structure prediction was retrieved using softberry web online tools ( http://linux1.softberry.com/berryPHTML?Topic=protcomppl&group=programs&group=Proloc (accessed on 2 April 2021)) and finally used to predict the subcellular localization of 79 ClPRX proteins.



    Similar Products

    protein secondary structure prediction web online tools  (Softberry Inc)
    90
    Softberry Inc protein secondary structure prediction web online tools
    The detailed genes information of ClPRXs.
    Protein Secondary Structure Prediction Web Online Tools, supplied by Softberry Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/protein+secondary+structure+prediction+web+online+tools/protein+localization+prediction+tool/pmc08775647-303-10-17
    Average 90 stars, based on 1 article reviews
    protein secondary structure prediction web online tools - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    The detailed genes information of ClPRXs.

    Journal: International Journal of Molecular Sciences

    Article Title: Genome-Wide Analysis of the Peroxidase Gene Family and Verification of Lignin Synthesis-Related Genes in Watermelon

    doi: 10.3390/ijms23020642

    Figure Lengend Snippet: The detailed genes information of ClPRXs.

    Article Snippet: Online information at http://h-s.p-443.npsa-prabi.ibcp.fr.neau.vpn358.com/cgi-bin/npsa_automat.pl?page=/NPSA/npsa_gor4.html (accessed on 2 April 2021) for protein secondary structure prediction was retrieved using softberry web online tools ( http://linux1.softberry.com/berryPHTML?Topic=protcomppl&group=programs&group=Proloc (accessed on 2 April 2021)) and finally used to predict the subcellular localization of 79 ClPRX proteins.

    Techniques: Molecular Weight

    Structural characteristics of ClPRX protein. ( A ) Schematic diagram of the primary structure of the class III peroxidase. The green boxes at the front and back signify the N-terminal signal peptide (SP) and c-terminal extension domain (CT). The middle three boxes represent the highly conserved domain: box I is the distal-heme-binding site domain; box Ⅱ is the unknown functional domain; box Ⅲ is the proximal-heme-binding site domain. The gray area with obvious variation was assumed to be a variable domain responsible for the specific catalytic function of peroxidase. The highly conserved distal histidine (Hd) and proximal histidine (HP) are heme-binding sites represented by green bars. Eight cysteines (C1–C8) are key amino acids that form disulfide bonds to form the secondary structure of peroxidase, which are represented by yellow solid circles. The four conserved disulfide bonds formed are shown as black lines in plane. ( B ) represents the four conserved domains and site location information of the third type of peroxidase, which are marked on the amino acid sequence with four different colors, and the 3D model of the structure of the four domains is displayed, the yellow part being the functional site. ( C ) is the comparison results of 7 groups of ClPRX protein sequences.

    Journal: International Journal of Molecular Sciences

    Article Title: Genome-Wide Analysis of the Peroxidase Gene Family and Verification of Lignin Synthesis-Related Genes in Watermelon

    doi: 10.3390/ijms23020642

    Figure Lengend Snippet: Structural characteristics of ClPRX protein. ( A ) Schematic diagram of the primary structure of the class III peroxidase. The green boxes at the front and back signify the N-terminal signal peptide (SP) and c-terminal extension domain (CT). The middle three boxes represent the highly conserved domain: box I is the distal-heme-binding site domain; box Ⅱ is the unknown functional domain; box Ⅲ is the proximal-heme-binding site domain. The gray area with obvious variation was assumed to be a variable domain responsible for the specific catalytic function of peroxidase. The highly conserved distal histidine (Hd) and proximal histidine (HP) are heme-binding sites represented by green bars. Eight cysteines (C1–C8) are key amino acids that form disulfide bonds to form the secondary structure of peroxidase, which are represented by yellow solid circles. The four conserved disulfide bonds formed are shown as black lines in plane. ( B ) represents the four conserved domains and site location information of the third type of peroxidase, which are marked on the amino acid sequence with four different colors, and the 3D model of the structure of the four domains is displayed, the yellow part being the functional site. ( C ) is the comparison results of 7 groups of ClPRX protein sequences.

    Article Snippet: Online information at http://h-s.p-443.npsa-prabi.ibcp.fr.neau.vpn358.com/cgi-bin/npsa_automat.pl?page=/NPSA/npsa_gor4.html (accessed on 2 April 2021) for protein secondary structure prediction was retrieved using softberry web online tools ( http://linux1.softberry.com/berryPHTML?Topic=protcomppl&group=programs&group=Proloc (accessed on 2 April 2021)) and finally used to predict the subcellular localization of 79 ClPRX proteins.

    Techniques: Binding Assay, Functional Assay, Sequencing, Comparison