alphafold model Search Results


alphafold models  (Gallus BioPharmaceuticals)
90
Gallus BioPharmaceuticals alphafold models
<t>AlphaFold</t> prediction of most parsimonious tentative structure of the F-keratin tetrameric N-block, AA 1-–52 (4 × 52 = 208 residues). Monomers are color-coded by chain (blue, red, green, yellow). Cysteine residues are displayed in a ball-stick view with standard colors. (a) Side view, staircase arrangement of helical β -strands in levels 1-8 (highlighted in the colors of adjacent β -strands) in the axial direction. Chain orientations of individual monomers are indicated by the respective AA number. (b) side view 90° turned, β -strands are rotationally staggered by an average horizontal angle of 11.125°per β -strand. The 8th strand is rotated 89°against the 1st strand in Pavo cristatus . The distance between the sandwiched sheets is 1.0-1.2 nm. Note that the polypeptide backbones of the four monomers are intertwined between strands in levels 4 and 5. (c) Axial view. (d) Equatorial cross-section of (a), corresponding to (c). AA 37-S, 38-T, and 47-I sit in the equatorial plane.
Alphafold Models, supplied by Gallus BioPharmaceuticals, 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
alphafold models - by Bioz Stars, 2026-06
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superimposition of alphafold models with corresponding solved structures  (Schrodinger LLC)
90
Schrodinger LLC superimposition of alphafold models with corresponding solved structures
<t>AlphaFold</t> prediction of most parsimonious tentative structure of the F-keratin tetrameric N-block, AA 1-–52 (4 × 52 = 208 residues). Monomers are color-coded by chain (blue, red, green, yellow). Cysteine residues are displayed in a ball-stick view with standard colors. (a) Side view, staircase arrangement of helical β -strands in levels 1-8 (highlighted in the colors of adjacent β -strands) in the axial direction. Chain orientations of individual monomers are indicated by the respective AA number. (b) side view 90° turned, β -strands are rotationally staggered by an average horizontal angle of 11.125°per β -strand. The 8th strand is rotated 89°against the 1st strand in Pavo cristatus . The distance between the sandwiched sheets is 1.0-1.2 nm. Note that the polypeptide backbones of the four monomers are intertwined between strands in levels 4 and 5. (c) Axial view. (d) Equatorial cross-section of (a), corresponding to (c). AA 37-S, 38-T, and 47-I sit in the equatorial plane.
Superimposition Of Alphafold Models With Corresponding Solved Structures, 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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Average 90 stars, based on 1 article reviews
superimposition of alphafold models with corresponding solved structures - by Bioz Stars, 2026-06
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alphafold model  (MBL Life science)
90
MBL Life science alphafold model
<t>AlphaFold</t> prediction of most parsimonious tentative structure of the F-keratin tetrameric N-block, AA 1-–52 (4 × 52 = 208 residues). Monomers are color-coded by chain (blue, red, green, yellow). Cysteine residues are displayed in a ball-stick view with standard colors. (a) Side view, staircase arrangement of helical β -strands in levels 1-8 (highlighted in the colors of adjacent β -strands) in the axial direction. Chain orientations of individual monomers are indicated by the respective AA number. (b) side view 90° turned, β -strands are rotationally staggered by an average horizontal angle of 11.125°per β -strand. The 8th strand is rotated 89°against the 1st strand in Pavo cristatus . The distance between the sandwiched sheets is 1.0-1.2 nm. Note that the polypeptide backbones of the four monomers are intertwined between strands in levels 4 and 5. (c) Axial view. (d) Equatorial cross-section of (a), corresponding to (c). AA 37-S, 38-T, and 47-I sit in the equatorial plane.
Alphafold Model, supplied by MBL Life science, 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/result/alphafold model/product/MBL Life science
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alphafold model - by Bioz Stars, 2026-06
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alphafold model for syngap α2 isoform-1  (SynGap Research Fund Inc)
90
SynGap Research Fund Inc alphafold model for syngap α2 isoform-1
<t>AlphaFold</t> prediction of most parsimonious tentative structure of the F-keratin tetrameric N-block, AA 1-–52 (4 × 52 = 208 residues). Monomers are color-coded by chain (blue, red, green, yellow). Cysteine residues are displayed in a ball-stick view with standard colors. (a) Side view, staircase arrangement of helical β -strands in levels 1-8 (highlighted in the colors of adjacent β -strands) in the axial direction. Chain orientations of individual monomers are indicated by the respective AA number. (b) side view 90° turned, β -strands are rotationally staggered by an average horizontal angle of 11.125°per β -strand. The 8th strand is rotated 89°against the 1st strand in Pavo cristatus . The distance between the sandwiched sheets is 1.0-1.2 nm. Note that the polypeptide backbones of the four monomers are intertwined between strands in levels 4 and 5. (c) Axial view. (d) Equatorial cross-section of (a), corresponding to (c). AA 37-S, 38-T, and 47-I sit in the equatorial plane.
Alphafold Model For Syngap α2 Isoform 1, supplied by SynGap Research Fund 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/result/alphafold model for syngap α2 isoform-1/product/SynGap Research Fund Inc
Average 90 stars, based on 1 article reviews
alphafold model for syngap α2 isoform-1 - by Bioz Stars, 2026-06
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alphafold 3 model  (Modelcraft Company Inc)
90
Modelcraft Company Inc alphafold 3 model
<t>AlphaFold</t> prediction of most parsimonious tentative structure of the F-keratin tetrameric N-block, AA 1-–52 (4 × 52 = 208 residues). Monomers are color-coded by chain (blue, red, green, yellow). Cysteine residues are displayed in a ball-stick view with standard colors. (a) Side view, staircase arrangement of helical β -strands in levels 1-8 (highlighted in the colors of adjacent β -strands) in the axial direction. Chain orientations of individual monomers are indicated by the respective AA number. (b) side view 90° turned, β -strands are rotationally staggered by an average horizontal angle of 11.125°per β -strand. The 8th strand is rotated 89°against the 1st strand in Pavo cristatus . The distance between the sandwiched sheets is 1.0-1.2 nm. Note that the polypeptide backbones of the four monomers are intertwined between strands in levels 4 and 5. (c) Axial view. (d) Equatorial cross-section of (a), corresponding to (c). AA 37-S, 38-T, and 47-I sit in the equatorial plane.
Alphafold 3 Model, supplied by Modelcraft Company 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/result/alphafold 3 model/product/Modelcraft Company Inc
Average 90 stars, based on 1 article reviews
alphafold 3 model - by Bioz Stars, 2026-06
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alphafold 3 modelling  (HealthTech Connex Inc)
90
HealthTech Connex Inc alphafold 3 modelling
<t>AlphaFold</t> prediction of most parsimonious tentative structure of the F-keratin tetrameric N-block, AA 1-–52 (4 × 52 = 208 residues). Monomers are color-coded by chain (blue, red, green, yellow). Cysteine residues are displayed in a ball-stick view with standard colors. (a) Side view, staircase arrangement of helical β -strands in levels 1-8 (highlighted in the colors of adjacent β -strands) in the axial direction. Chain orientations of individual monomers are indicated by the respective AA number. (b) side view 90° turned, β -strands are rotationally staggered by an average horizontal angle of 11.125°per β -strand. The 8th strand is rotated 89°against the 1st strand in Pavo cristatus . The distance between the sandwiched sheets is 1.0-1.2 nm. Note that the polypeptide backbones of the four monomers are intertwined between strands in levels 4 and 5. (c) Axial view. (d) Equatorial cross-section of (a), corresponding to (c). AA 37-S, 38-T, and 47-I sit in the equatorial plane.
Alphafold 3 Modelling, 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
https://www.bioz.com/result/alphafold 3 modelling/product/HealthTech Connex Inc
Average 90 stars, based on 1 article reviews
alphafold 3 modelling - by Bioz Stars, 2026-06
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alphafold-predicted three-dimensional models  (Agenta Biotechnologies)
90
Agenta Biotechnologies alphafold-predicted three-dimensional models
<t>AlphaFold</t> prediction of most parsimonious tentative structure of the F-keratin tetrameric N-block, AA 1-–52 (4 × 52 = 208 residues). Monomers are color-coded by chain (blue, red, green, yellow). Cysteine residues are displayed in a ball-stick view with standard colors. (a) Side view, staircase arrangement of helical β -strands in levels 1-8 (highlighted in the colors of adjacent β -strands) in the axial direction. Chain orientations of individual monomers are indicated by the respective AA number. (b) side view 90° turned, β -strands are rotationally staggered by an average horizontal angle of 11.125°per β -strand. The 8th strand is rotated 89°against the 1st strand in Pavo cristatus . The distance between the sandwiched sheets is 1.0-1.2 nm. Note that the polypeptide backbones of the four monomers are intertwined between strands in levels 4 and 5. (c) Axial view. (d) Equatorial cross-section of (a), corresponding to (c). AA 37-S, 38-T, and 47-I sit in the equatorial plane.
Alphafold Predicted Three Dimensional Models, supplied by Agenta Biotechnologies, 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/result/alphafold-predicted three-dimensional models/product/Agenta Biotechnologies
Average 90 stars, based on 1 article reviews
alphafold-predicted three-dimensional models - by Bioz Stars, 2026-06
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alphafold models of the interpro family with id: ipr004836  (InterPro Inc)
90
InterPro Inc alphafold models of the interpro family with id: ipr004836
<t>AlphaFold</t> prediction of most parsimonious tentative structure of the F-keratin tetrameric N-block, AA 1-–52 (4 × 52 = 208 residues). Monomers are color-coded by chain (blue, red, green, yellow). Cysteine residues are displayed in a ball-stick view with standard colors. (a) Side view, staircase arrangement of helical β -strands in levels 1-8 (highlighted in the colors of adjacent β -strands) in the axial direction. Chain orientations of individual monomers are indicated by the respective AA number. (b) side view 90° turned, β -strands are rotationally staggered by an average horizontal angle of 11.125°per β -strand. The 8th strand is rotated 89°against the 1st strand in Pavo cristatus . The distance between the sandwiched sheets is 1.0-1.2 nm. Note that the polypeptide backbones of the four monomers are intertwined between strands in levels 4 and 5. (c) Axial view. (d) Equatorial cross-section of (a), corresponding to (c). AA 37-S, 38-T, and 47-I sit in the equatorial plane.
Alphafold Models Of The Interpro Family With Id: Ipr004836, 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
https://www.bioz.com/result/alphafold models of the interpro family with id: ipr004836/product/InterPro Inc
Average 90 stars, based on 1 article reviews
alphafold models of the interpro family with id: ipr004836 - by Bioz Stars, 2026-06
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visualization and superimposition of alphafold models and x-ray structural data  (Schrodinger LLC)
90
Schrodinger LLC visualization and superimposition of alphafold models and x-ray structural data
<t>AlphaFold</t> prediction of most parsimonious tentative structure of the F-keratin tetrameric N-block, AA 1-–52 (4 × 52 = 208 residues). Monomers are color-coded by chain (blue, red, green, yellow). Cysteine residues are displayed in a ball-stick view with standard colors. (a) Side view, staircase arrangement of helical β -strands in levels 1-8 (highlighted in the colors of adjacent β -strands) in the axial direction. Chain orientations of individual monomers are indicated by the respective AA number. (b) side view 90° turned, β -strands are rotationally staggered by an average horizontal angle of 11.125°per β -strand. The 8th strand is rotated 89°against the 1st strand in Pavo cristatus . The distance between the sandwiched sheets is 1.0-1.2 nm. Note that the polypeptide backbones of the four monomers are intertwined between strands in levels 4 and 5. (c) Axial view. (d) Equatorial cross-section of (a), corresponding to (c). AA 37-S, 38-T, and 47-I sit in the equatorial plane.
Visualization And Superimposition Of Alphafold Models And X Ray Structural Data, 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
https://www.bioz.com/result/visualization and superimposition of alphafold models and x-ray structural data/product/Schrodinger LLC
Average 90 stars, based on 1 article reviews
visualization and superimposition of alphafold models and x-ray structural data - by Bioz Stars, 2026-06
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alphafold 3 model  (Deepmind Technologies Ltd)
86
Deepmind Technologies Ltd alphafold 3 model
<t>AlphaFold</t> prediction of most parsimonious tentative structure of the F-keratin tetrameric N-block, AA 1-–52 (4 × 52 = 208 residues). Monomers are color-coded by chain (blue, red, green, yellow). Cysteine residues are displayed in a ball-stick view with standard colors. (a) Side view, staircase arrangement of helical β -strands in levels 1-8 (highlighted in the colors of adjacent β -strands) in the axial direction. Chain orientations of individual monomers are indicated by the respective AA number. (b) side view 90° turned, β -strands are rotationally staggered by an average horizontal angle of 11.125°per β -strand. The 8th strand is rotated 89°against the 1st strand in Pavo cristatus . The distance between the sandwiched sheets is 1.0-1.2 nm. Note that the polypeptide backbones of the four monomers are intertwined between strands in levels 4 and 5. (c) Axial view. (d) Equatorial cross-section of (a), corresponding to (c). AA 37-S, 38-T, and 47-I sit in the equatorial plane.
Alphafold 3 Model, supplied by Deepmind Technologies Ltd, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/alphafold 3 model/product/Deepmind Technologies Ltd
Average 86 stars, based on 1 article reviews
alphafold 3 model - by Bioz Stars, 2026-06
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alphafold model af q96du3 f1  (Deepmind Technologies Ltd)
86
Deepmind Technologies Ltd alphafold model af q96du3 f1
<t>AlphaFold</t> prediction of most parsimonious tentative structure of the F-keratin tetrameric N-block, AA 1-–52 (4 × 52 = 208 residues). Monomers are color-coded by chain (blue, red, green, yellow). Cysteine residues are displayed in a ball-stick view with standard colors. (a) Side view, staircase arrangement of helical β -strands in levels 1-8 (highlighted in the colors of adjacent β -strands) in the axial direction. Chain orientations of individual monomers are indicated by the respective AA number. (b) side view 90° turned, β -strands are rotationally staggered by an average horizontal angle of 11.125°per β -strand. The 8th strand is rotated 89°against the 1st strand in Pavo cristatus . The distance between the sandwiched sheets is 1.0-1.2 nm. Note that the polypeptide backbones of the four monomers are intertwined between strands in levels 4 and 5. (c) Axial view. (d) Equatorial cross-section of (a), corresponding to (c). AA 37-S, 38-T, and 47-I sit in the equatorial plane.
Alphafold Model Af Q96du3 F1, supplied by Deepmind Technologies Ltd, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/alphafold model af q96du3 f1/product/Deepmind Technologies Ltd
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alphafold dm model  (Deepmind Technologies Ltd)
86
Deepmind Technologies Ltd alphafold dm model
<t>AlphaFold</t> prediction of most parsimonious tentative structure of the F-keratin tetrameric N-block, AA 1-–52 (4 × 52 = 208 residues). Monomers are color-coded by chain (blue, red, green, yellow). Cysteine residues are displayed in a ball-stick view with standard colors. (a) Side view, staircase arrangement of helical β -strands in levels 1-8 (highlighted in the colors of adjacent β -strands) in the axial direction. Chain orientations of individual monomers are indicated by the respective AA number. (b) side view 90° turned, β -strands are rotationally staggered by an average horizontal angle of 11.125°per β -strand. The 8th strand is rotated 89°against the 1st strand in Pavo cristatus . The distance between the sandwiched sheets is 1.0-1.2 nm. Note that the polypeptide backbones of the four monomers are intertwined between strands in levels 4 and 5. (c) Axial view. (d) Equatorial cross-section of (a), corresponding to (c). AA 37-S, 38-T, and 47-I sit in the equatorial plane.
Alphafold Dm Model, supplied by Deepmind Technologies Ltd, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


AlphaFold prediction of most parsimonious tentative structure of the F-keratin tetrameric N-block, AA 1-–52 (4 × 52 = 208 residues). Monomers are color-coded by chain (blue, red, green, yellow). Cysteine residues are displayed in a ball-stick view with standard colors. (a) Side view, staircase arrangement of helical β -strands in levels 1-8 (highlighted in the colors of adjacent β -strands) in the axial direction. Chain orientations of individual monomers are indicated by the respective AA number. (b) side view 90° turned, β -strands are rotationally staggered by an average horizontal angle of 11.125°per β -strand. The 8th strand is rotated 89°against the 1st strand in Pavo cristatus . The distance between the sandwiched sheets is 1.0-1.2 nm. Note that the polypeptide backbones of the four monomers are intertwined between strands in levels 4 and 5. (c) Axial view. (d) Equatorial cross-section of (a), corresponding to (c). AA 37-S, 38-T, and 47-I sit in the equatorial plane.

Journal: bioRxiv

Article Title: Feather keratin in Pavo cristatus : A tentative structure

doi: 10.1101/2024.09.08.611866

Figure Lengend Snippet: AlphaFold prediction of most parsimonious tentative structure of the F-keratin tetrameric N-block, AA 1-–52 (4 × 52 = 208 residues). Monomers are color-coded by chain (blue, red, green, yellow). Cysteine residues are displayed in a ball-stick view with standard colors. (a) Side view, staircase arrangement of helical β -strands in levels 1-8 (highlighted in the colors of adjacent β -strands) in the axial direction. Chain orientations of individual monomers are indicated by the respective AA number. (b) side view 90° turned, β -strands are rotationally staggered by an average horizontal angle of 11.125°per β -strand. The 8th strand is rotated 89°against the 1st strand in Pavo cristatus . The distance between the sandwiched sheets is 1.0-1.2 nm. Note that the polypeptide backbones of the four monomers are intertwined between strands in levels 4 and 5. (c) Axial view. (d) Equatorial cross-section of (a), corresponding to (c). AA 37-S, 38-T, and 47-I sit in the equatorial plane.

Article Snippet: So far, according to AlphaFold models, C-block segments of Gallus gallus and Larus novaehollandiae lack such interfacial fit.

Techniques: Blocking Assay

AlphaFold prediction of the Pavo cristatus F-keratin tetrameric C-block, AA 81-–100 (4 × 20 = 80 residues). Monomers are color-coded by chain (blue, red, green, yellow). The four 98-Y and 12 cysteine residues are displayed in a ball-stick view with standard colors. Chain orientations of individual monomers are indicated by the respective amino acid number. (a) Side view, filament axis vertical. (b) The side view turned 90°around the filament axis. (c) Top view, along the filament axis. Note that each pair of β -strands forms one level; the arrangement is rectangular rather than square in the (x,y) plane. The direction of the β -strand arrows is from N-to C-terminus. (d) shows the outer aromates from the 81-FGYGFGGLGCF motif in the same view as (b).

Journal: bioRxiv

Article Title: Feather keratin in Pavo cristatus : A tentative structure

doi: 10.1101/2024.09.08.611866

Figure Lengend Snippet: AlphaFold prediction of the Pavo cristatus F-keratin tetrameric C-block, AA 81-–100 (4 × 20 = 80 residues). Monomers are color-coded by chain (blue, red, green, yellow). The four 98-Y and 12 cysteine residues are displayed in a ball-stick view with standard colors. Chain orientations of individual monomers are indicated by the respective amino acid number. (a) Side view, filament axis vertical. (b) The side view turned 90°around the filament axis. (c) Top view, along the filament axis. Note that each pair of β -strands forms one level; the arrangement is rectangular rather than square in the (x,y) plane. The direction of the β -strand arrows is from N-to C-terminus. (d) shows the outer aromates from the 81-FGYGFGGLGCF motif in the same view as (b).

Article Snippet: So far, according to AlphaFold models, C-block segments of Gallus gallus and Larus novaehollandiae lack such interfacial fit.

Techniques: Blocking Assay