protein structure prediction tools Search Results


90
GenScript corporation protein subcellular localization prediction tool
Protein Subcellular Localization Prediction Tool, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Innovagen AB protein solubility prediction tool
Protein Solubility Prediction Tool, supplied by Innovagen AB, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Lawrence Livermore National Security LLC protein structure prediction center
Protein Structure Prediction Center, supplied by Lawrence Livermore National Security LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Schrodinger LLC three-dimensional protein structure prediction program prime
Three Dimensional Protein Structure Prediction Program Prime, supplied by Schrodinger LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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CLC Bio protein secondary structure prediction
Comparison of BnMicEmUP3 protein to PEND proteins. (A) Alignment of PEND homologs to BnMicEmUP3 protein from various plant species. PEND sequences have been identified in various angiosperms by . Sources of sequences: P. sat ( Pisum sativa , PEND, genome: AB189736); B. nap ( B. napus : GSBF1, cDNA: X91138); B. nap1 ( B. napus , genome: AB189734); B. nap2 ( B. napus , genome: AB189735); A. tha ( A. thaliana , genome: AL094711); G. max ( G. max , EST:BM308592); M. tru ( Medicago truncatula , ESTs: BG644842); L. esc ( Lycopersicon esculentum , ESTs: BE450861); H. vul ( Hordeum vulgare , ESTs: AV833513); O. sat ( Oryza sativa , genome: EST: AK106548); C. sat ( Cucumis sativus , genome: AB189737); and P. yed ( Prunus yedoensis , genome: AB189738) BnMicEmUP3 ( B. napus , genome: HQ660216). The consensus residues are colored according to: red, hydrophobic; purple, basic; green, hydrophilic; and blue, acidic. Highlighted residues show identical (dark red) or similar (gray) amino acids <t>between</t> <t>BnMicEmUP</t> bZIP domains and bZIP domains of PEND proteins. Additional common structural domains include a short pre-sequence (black), an N-terminal DNA-binding domain (dark red), central repeat domain (gray), and C-terminal transmembrane domains (yellow). (B) Phylogenetic tree of PEND homologs. The phylogenetic tree was constructed by the neighbor-joining method with 100 bootstrap replicates using <t>CLC</t> software. The numbers on branches show bootstrap confidence levels based on 100 bootstrap trials.
Protein Secondary Structure Prediction, supplied by CLC Bio, 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+structure+prediction+tools/pmc07845737-186-1-7?v=CLC+Bio
Average 90 stars, based on 1 article reviews
protein secondary structure prediction - by Bioz Stars, 2026-08
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GenScript corporation protein subcellular localization prediction tool psort
Comparison of BnMicEmUP3 protein to PEND proteins. (A) Alignment of PEND homologs to BnMicEmUP3 protein from various plant species. PEND sequences have been identified in various angiosperms by . Sources of sequences: P. sat ( Pisum sativa , PEND, genome: AB189736); B. nap ( B. napus : GSBF1, cDNA: X91138); B. nap1 ( B. napus , genome: AB189734); B. nap2 ( B. napus , genome: AB189735); A. tha ( A. thaliana , genome: AL094711); G. max ( G. max , EST:BM308592); M. tru ( Medicago truncatula , ESTs: BG644842); L. esc ( Lycopersicon esculentum , ESTs: BE450861); H. vul ( Hordeum vulgare , ESTs: AV833513); O. sat ( Oryza sativa , genome: EST: AK106548); C. sat ( Cucumis sativus , genome: AB189737); and P. yed ( Prunus yedoensis , genome: AB189738) BnMicEmUP3 ( B. napus , genome: HQ660216). The consensus residues are colored according to: red, hydrophobic; purple, basic; green, hydrophilic; and blue, acidic. Highlighted residues show identical (dark red) or similar (gray) amino acids <t>between</t> <t>BnMicEmUP</t> bZIP domains and bZIP domains of PEND proteins. Additional common structural domains include a short pre-sequence (black), an N-terminal DNA-binding domain (dark red), central repeat domain (gray), and C-terminal transmembrane domains (yellow). (B) Phylogenetic tree of PEND homologs. The phylogenetic tree was constructed by the neighbor-joining method with 100 bootstrap replicates using <t>CLC</t> software. The numbers on branches show bootstrap confidence levels based on 100 bootstrap trials.
Protein Subcellular Localization Prediction Tool Psort, supplied by GenScript corporation, 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+structure+prediction+tools/pm37972007-234-1-7?v=GenScript+corporation
Average 90 stars, based on 1 article reviews
protein subcellular localization prediction tool psort - by Bioz Stars, 2026-08
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90
Applied Bioinformatics protein structure prediction
Comparison of BnMicEmUP3 protein to PEND proteins. (A) Alignment of PEND homologs to BnMicEmUP3 protein from various plant species. PEND sequences have been identified in various angiosperms by . Sources of sequences: P. sat ( Pisum sativa , PEND, genome: AB189736); B. nap ( B. napus : GSBF1, cDNA: X91138); B. nap1 ( B. napus , genome: AB189734); B. nap2 ( B. napus , genome: AB189735); A. tha ( A. thaliana , genome: AL094711); G. max ( G. max , EST:BM308592); M. tru ( Medicago truncatula , ESTs: BG644842); L. esc ( Lycopersicon esculentum , ESTs: BE450861); H. vul ( Hordeum vulgare , ESTs: AV833513); O. sat ( Oryza sativa , genome: EST: AK106548); C. sat ( Cucumis sativus , genome: AB189737); and P. yed ( Prunus yedoensis , genome: AB189738) BnMicEmUP3 ( B. napus , genome: HQ660216). The consensus residues are colored according to: red, hydrophobic; purple, basic; green, hydrophilic; and blue, acidic. Highlighted residues show identical (dark red) or similar (gray) amino acids <t>between</t> <t>BnMicEmUP</t> bZIP domains and bZIP domains of PEND proteins. Additional common structural domains include a short pre-sequence (black), an N-terminal DNA-binding domain (dark red), central repeat domain (gray), and C-terminal transmembrane domains (yellow). (B) Phylogenetic tree of PEND homologs. The phylogenetic tree was constructed by the neighbor-joining method with 100 bootstrap replicates using <t>CLC</t> software. The numbers on branches show bootstrap confidence levels based on 100 bootstrap trials.
Protein Structure Prediction, supplied by Applied Bioinformatics, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
protein structure prediction - by Bioz Stars, 2026-08
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Interactive Biosoftware protein-function prediction tools
Comparison of BnMicEmUP3 protein to PEND proteins. (A) Alignment of PEND homologs to BnMicEmUP3 protein from various plant species. PEND sequences have been identified in various angiosperms by . Sources of sequences: P. sat ( Pisum sativa , PEND, genome: AB189736); B. nap ( B. napus : GSBF1, cDNA: X91138); B. nap1 ( B. napus , genome: AB189734); B. nap2 ( B. napus , genome: AB189735); A. tha ( A. thaliana , genome: AL094711); G. max ( G. max , EST:BM308592); M. tru ( Medicago truncatula , ESTs: BG644842); L. esc ( Lycopersicon esculentum , ESTs: BE450861); H. vul ( Hordeum vulgare , ESTs: AV833513); O. sat ( Oryza sativa , genome: EST: AK106548); C. sat ( Cucumis sativus , genome: AB189737); and P. yed ( Prunus yedoensis , genome: AB189738) BnMicEmUP3 ( B. napus , genome: HQ660216). The consensus residues are colored according to: red, hydrophobic; purple, basic; green, hydrophilic; and blue, acidic. Highlighted residues show identical (dark red) or similar (gray) amino acids <t>between</t> <t>BnMicEmUP</t> bZIP domains and bZIP domains of PEND proteins. Additional common structural domains include a short pre-sequence (black), an N-terminal DNA-binding domain (dark red), central repeat domain (gray), and C-terminal transmembrane domains (yellow). (B) Phylogenetic tree of PEND homologs. The phylogenetic tree was constructed by the neighbor-joining method with 100 bootstrap replicates using <t>CLC</t> software. The numbers on branches show bootstrap confidence levels based on 100 bootstrap trials.
Protein Function Prediction Tools, supplied by Interactive Biosoftware, 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+structure+prediction+tools/pmc06127642-110-19-10?v=Interactive+Biosoftware
Average 90 stars, based on 1 article reviews
protein-function prediction tools - by Bioz Stars, 2026-08
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HealthTech Connex Inc structure prediction of non-classical secretory proteins tmhmm
Comparison of BnMicEmUP3 protein to PEND proteins. (A) Alignment of PEND homologs to BnMicEmUP3 protein from various plant species. PEND sequences have been identified in various angiosperms by . Sources of sequences: P. sat ( Pisum sativa , PEND, genome: AB189736); B. nap ( B. napus : GSBF1, cDNA: X91138); B. nap1 ( B. napus , genome: AB189734); B. nap2 ( B. napus , genome: AB189735); A. tha ( A. thaliana , genome: AL094711); G. max ( G. max , EST:BM308592); M. tru ( Medicago truncatula , ESTs: BG644842); L. esc ( Lycopersicon esculentum , ESTs: BE450861); H. vul ( Hordeum vulgare , ESTs: AV833513); O. sat ( Oryza sativa , genome: EST: AK106548); C. sat ( Cucumis sativus , genome: AB189737); and P. yed ( Prunus yedoensis , genome: AB189738) BnMicEmUP3 ( B. napus , genome: HQ660216). The consensus residues are colored according to: red, hydrophobic; purple, basic; green, hydrophilic; and blue, acidic. Highlighted residues show identical (dark red) or similar (gray) amino acids <t>between</t> <t>BnMicEmUP</t> bZIP domains and bZIP domains of PEND proteins. Additional common structural domains include a short pre-sequence (black), an N-terminal DNA-binding domain (dark red), central repeat domain (gray), and C-terminal transmembrane domains (yellow). (B) Phylogenetic tree of PEND homologs. The phylogenetic tree was constructed by the neighbor-joining method with 100 bootstrap replicates using <t>CLC</t> software. The numbers on branches show bootstrap confidence levels based on 100 bootstrap trials.
Structure Prediction Of Non Classical Secretory Proteins Tmhmm, supplied by HealthTech Connex Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
structure prediction of non-classical secretory proteins tmhmm - by Bioz Stars, 2026-08
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InterPro Inc protein prediction tool interpro scan
Comparison of BnMicEmUP3 protein to PEND proteins. (A) Alignment of PEND homologs to BnMicEmUP3 protein from various plant species. PEND sequences have been identified in various angiosperms by . Sources of sequences: P. sat ( Pisum sativa , PEND, genome: AB189736); B. nap ( B. napus : GSBF1, cDNA: X91138); B. nap1 ( B. napus , genome: AB189734); B. nap2 ( B. napus , genome: AB189735); A. tha ( A. thaliana , genome: AL094711); G. max ( G. max , EST:BM308592); M. tru ( Medicago truncatula , ESTs: BG644842); L. esc ( Lycopersicon esculentum , ESTs: BE450861); H. vul ( Hordeum vulgare , ESTs: AV833513); O. sat ( Oryza sativa , genome: EST: AK106548); C. sat ( Cucumis sativus , genome: AB189737); and P. yed ( Prunus yedoensis , genome: AB189738) BnMicEmUP3 ( B. napus , genome: HQ660216). The consensus residues are colored according to: red, hydrophobic; purple, basic; green, hydrophilic; and blue, acidic. Highlighted residues show identical (dark red) or similar (gray) amino acids <t>between</t> <t>BnMicEmUP</t> bZIP domains and bZIP domains of PEND proteins. Additional common structural domains include a short pre-sequence (black), an N-terminal DNA-binding domain (dark red), central repeat domain (gray), and C-terminal transmembrane domains (yellow). (B) Phylogenetic tree of PEND homologs. The phylogenetic tree was constructed by the neighbor-joining method with 100 bootstrap replicates using <t>CLC</t> software. The numbers on branches show bootstrap confidence levels based on 100 bootstrap trials.
Protein Prediction Tool Interpro Scan, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Molegro ApS structure protein alignment tool
Comparison of BnMicEmUP3 protein to PEND proteins. (A) Alignment of PEND homologs to BnMicEmUP3 protein from various plant species. PEND sequences have been identified in various angiosperms by . Sources of sequences: P. sat ( Pisum sativa , PEND, genome: AB189736); B. nap ( B. napus : GSBF1, cDNA: X91138); B. nap1 ( B. napus , genome: AB189734); B. nap2 ( B. napus , genome: AB189735); A. tha ( A. thaliana , genome: AL094711); G. max ( G. max , EST:BM308592); M. tru ( Medicago truncatula , ESTs: BG644842); L. esc ( Lycopersicon esculentum , ESTs: BE450861); H. vul ( Hordeum vulgare , ESTs: AV833513); O. sat ( Oryza sativa , genome: EST: AK106548); C. sat ( Cucumis sativus , genome: AB189737); and P. yed ( Prunus yedoensis , genome: AB189738) BnMicEmUP3 ( B. napus , genome: HQ660216). The consensus residues are colored according to: red, hydrophobic; purple, basic; green, hydrophilic; and blue, acidic. Highlighted residues show identical (dark red) or similar (gray) amino acids <t>between</t> <t>BnMicEmUP</t> bZIP domains and bZIP domains of PEND proteins. Additional common structural domains include a short pre-sequence (black), an N-terminal DNA-binding domain (dark red), central repeat domain (gray), and C-terminal transmembrane domains (yellow). (B) Phylogenetic tree of PEND homologs. The phylogenetic tree was constructed by the neighbor-joining method with 100 bootstrap replicates using <t>CLC</t> software. The numbers on branches show bootstrap confidence levels based on 100 bootstrap trials.
Structure Protein Alignment Tool, supplied by Molegro ApS, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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InterPro Inc protein prediction tool
Comparison of BnMicEmUP3 protein to PEND proteins. (A) Alignment of PEND homologs to BnMicEmUP3 protein from various plant species. PEND sequences have been identified in various angiosperms by . Sources of sequences: P. sat ( Pisum sativa , PEND, genome: AB189736); B. nap ( B. napus : GSBF1, cDNA: X91138); B. nap1 ( B. napus , genome: AB189734); B. nap2 ( B. napus , genome: AB189735); A. tha ( A. thaliana , genome: AL094711); G. max ( G. max , EST:BM308592); M. tru ( Medicago truncatula , ESTs: BG644842); L. esc ( Lycopersicon esculentum , ESTs: BE450861); H. vul ( Hordeum vulgare , ESTs: AV833513); O. sat ( Oryza sativa , genome: EST: AK106548); C. sat ( Cucumis sativus , genome: AB189737); and P. yed ( Prunus yedoensis , genome: AB189738) BnMicEmUP3 ( B. napus , genome: HQ660216). The consensus residues are colored according to: red, hydrophobic; purple, basic; green, hydrophilic; and blue, acidic. Highlighted residues show identical (dark red) or similar (gray) amino acids <t>between</t> <t>BnMicEmUP</t> bZIP domains and bZIP domains of PEND proteins. Additional common structural domains include a short pre-sequence (black), an N-terminal DNA-binding domain (dark red), central repeat domain (gray), and C-terminal transmembrane domains (yellow). (B) Phylogenetic tree of PEND homologs. The phylogenetic tree was constructed by the neighbor-joining method with 100 bootstrap replicates using <t>CLC</t> software. The numbers on branches show bootstrap confidence levels based on 100 bootstrap trials.
Protein Prediction Tool, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
protein prediction tool - by Bioz Stars, 2026-08
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Image Search Results


Comparison of BnMicEmUP3 protein to PEND proteins. (A) Alignment of PEND homologs to BnMicEmUP3 protein from various plant species. PEND sequences have been identified in various angiosperms by . Sources of sequences: P. sat ( Pisum sativa , PEND, genome: AB189736); B. nap ( B. napus : GSBF1, cDNA: X91138); B. nap1 ( B. napus , genome: AB189734); B. nap2 ( B. napus , genome: AB189735); A. tha ( A. thaliana , genome: AL094711); G. max ( G. max , EST:BM308592); M. tru ( Medicago truncatula , ESTs: BG644842); L. esc ( Lycopersicon esculentum , ESTs: BE450861); H. vul ( Hordeum vulgare , ESTs: AV833513); O. sat ( Oryza sativa , genome: EST: AK106548); C. sat ( Cucumis sativus , genome: AB189737); and P. yed ( Prunus yedoensis , genome: AB189738) BnMicEmUP3 ( B. napus , genome: HQ660216). The consensus residues are colored according to: red, hydrophobic; purple, basic; green, hydrophilic; and blue, acidic. Highlighted residues show identical (dark red) or similar (gray) amino acids between BnMicEmUP bZIP domains and bZIP domains of PEND proteins. Additional common structural domains include a short pre-sequence (black), an N-terminal DNA-binding domain (dark red), central repeat domain (gray), and C-terminal transmembrane domains (yellow). (B) Phylogenetic tree of PEND homologs. The phylogenetic tree was constructed by the neighbor-joining method with 100 bootstrap replicates using CLC software. The numbers on branches show bootstrap confidence levels based on 100 bootstrap trials.

Journal: Frontiers in Plant Science

Article Title: Identification, Gene Structure, and Expression of BnMicEmUP : A Gene Upregulated in Embryogenic Brassica napus Microspores

doi: 10.3389/fpls.2020.576008

Figure Lengend Snippet: Comparison of BnMicEmUP3 protein to PEND proteins. (A) Alignment of PEND homologs to BnMicEmUP3 protein from various plant species. PEND sequences have been identified in various angiosperms by . Sources of sequences: P. sat ( Pisum sativa , PEND, genome: AB189736); B. nap ( B. napus : GSBF1, cDNA: X91138); B. nap1 ( B. napus , genome: AB189734); B. nap2 ( B. napus , genome: AB189735); A. tha ( A. thaliana , genome: AL094711); G. max ( G. max , EST:BM308592); M. tru ( Medicago truncatula , ESTs: BG644842); L. esc ( Lycopersicon esculentum , ESTs: BE450861); H. vul ( Hordeum vulgare , ESTs: AV833513); O. sat ( Oryza sativa , genome: EST: AK106548); C. sat ( Cucumis sativus , genome: AB189737); and P. yed ( Prunus yedoensis , genome: AB189738) BnMicEmUP3 ( B. napus , genome: HQ660216). The consensus residues are colored according to: red, hydrophobic; purple, basic; green, hydrophilic; and blue, acidic. Highlighted residues show identical (dark red) or similar (gray) amino acids between BnMicEmUP bZIP domains and bZIP domains of PEND proteins. Additional common structural domains include a short pre-sequence (black), an N-terminal DNA-binding domain (dark red), central repeat domain (gray), and C-terminal transmembrane domains (yellow). (B) Phylogenetic tree of PEND homologs. The phylogenetic tree was constructed by the neighbor-joining method with 100 bootstrap replicates using CLC software. The numbers on branches show bootstrap confidence levels based on 100 bootstrap trials.

Article Snippet: The protein secondary structure prediction by CLC (CLC bio, Aarhus, Denmark) showed that the BnMicEmUP protein has a characteristic α -helical structure in the region that contains the leucine-rich repeats , which is the main structural motif found in bZIP proteins ( ).

Techniques: Comparison, Sequencing, Binding Assay, Construct, Software