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groundbreaking alphafold protein structure prediction tool  (Deepmind Technologies Ltd)

 
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    Deepmind Technologies Ltd groundbreaking alphafold protein structure prediction tool
    Groundbreaking Alphafold Protein Structure Prediction Tool, 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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    groundbreaking alphafold protein structure prediction tool  (Deepmind Technologies Ltd)
    86
    Deepmind Technologies Ltd groundbreaking alphafold protein structure prediction tool
    Groundbreaking Alphafold Protein Structure Prediction Tool, 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/product/protein+structures+predicted+by+alphafold/pm41725087-110-12-0?v=Deepmind+Technologies+Ltd
    Average 86 stars, based on 1 article reviews
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    alphafold protein structure database prediction server  (Deepmind Technologies Ltd)
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    Deepmind Technologies Ltd alphafold protein structure database prediction server
    CbbM_base: S162P, G422R, C6: H127V, M140A, K247A, H251A, Q392E, S432T + S162P, G422R, Ad1: H127V, K247A, H251A, Q392E, S432T, W114I + S162P, G422R. ( A ) Selectivity values of selected CbbM variants. (B ) Carboxylation rate constant ( k cat C ). ( C ) Oxygenation rate constant ( k cat O ). ( D ) Binding constant of CO2 in absence of oxygen, ( E ) of CO2 in air, ( F ) binding constant of O2. ( G ) Catalytic efficiency of carboxylation reaction in absence of air, ( H ) of carboxylation reaction in air, ( I ) catalytic efficiency of oxygenation reaction. All catalytic parameters were determined using a 14 CO2 fixation assay with four replicates. Statistical significance was assessed using a one-way ANOVA followed by Tukey’s multiple comparisons test ( J ) Visualization of important residues and active site in a CbbM model <t>(AlphaFold).</t> The dimers are shown in blue and yellow ( K ) Visualization of CbbM model displaying the location of residues mutated in variant Ad1. ( L ) Residue W114 (green) in CbbM constricts a tunnel (blue) in the dimer interface, connecting the two active sites.
    Alphafold Protein Structure Database Prediction Server, 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/product/protein+structures+predicted+by+alphafold/bio_rxiv__64898__2025__12__07__690893-355-14-20?v=Deepmind+Technologies+Ltd
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    alphafold protein structure database prediction server - by Bioz Stars, 2026-08
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    alphafold protein structure prediction  (Deepmind Technologies Ltd)
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    Deepmind Technologies Ltd alphafold protein structure prediction
    CbbM_base: S162P, G422R, C6: H127V, M140A, K247A, H251A, Q392E, S432T + S162P, G422R, Ad1: H127V, K247A, H251A, Q392E, S432T, W114I + S162P, G422R. ( A ) Selectivity values of selected CbbM variants. (B ) Carboxylation rate constant ( k cat C ). ( C ) Oxygenation rate constant ( k cat O ). ( D ) Binding constant of CO2 in absence of oxygen, ( E ) of CO2 in air, ( F ) binding constant of O2. ( G ) Catalytic efficiency of carboxylation reaction in absence of air, ( H ) of carboxylation reaction in air, ( I ) catalytic efficiency of oxygenation reaction. All catalytic parameters were determined using a 14 CO2 fixation assay with four replicates. Statistical significance was assessed using a one-way ANOVA followed by Tukey’s multiple comparisons test ( J ) Visualization of important residues and active site in a CbbM model <t>(AlphaFold).</t> The dimers are shown in blue and yellow ( K ) Visualization of CbbM model displaying the location of residues mutated in variant Ad1. ( L ) Residue W114 (green) in CbbM constricts a tunnel (blue) in the dimer interface, connecting the two active sites.
    Alphafold Protein Structure Prediction, 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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    Average 86 stars, based on 1 article reviews
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    alphafold protein structure prediction software  (Deepmind Technologies Ltd)
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    Deepmind Technologies Ltd alphafold protein structure prediction software
    CbbM_base: S162P, G422R, C6: H127V, M140A, K247A, H251A, Q392E, S432T + S162P, G422R, Ad1: H127V, K247A, H251A, Q392E, S432T, W114I + S162P, G422R. ( A ) Selectivity values of selected CbbM variants. (B ) Carboxylation rate constant ( k cat C ). ( C ) Oxygenation rate constant ( k cat O ). ( D ) Binding constant of CO2 in absence of oxygen, ( E ) of CO2 in air, ( F ) binding constant of O2. ( G ) Catalytic efficiency of carboxylation reaction in absence of air, ( H ) of carboxylation reaction in air, ( I ) catalytic efficiency of oxygenation reaction. All catalytic parameters were determined using a 14 CO2 fixation assay with four replicates. Statistical significance was assessed using a one-way ANOVA followed by Tukey’s multiple comparisons test ( J ) Visualization of important residues and active site in a CbbM model <t>(AlphaFold).</t> The dimers are shown in blue and yellow ( K ) Visualization of CbbM model displaying the location of residues mutated in variant Ad1. ( L ) Residue W114 (green) in CbbM constricts a tunnel (blue) in the dimer interface, connecting the two active sites.
    Alphafold Protein Structure Prediction Software, supplied by Deepmind Technologies Ltd, 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+structures+predicted+by+alphafold/pmc11754571-751-12-19?v=Deepmind+Technologies+Ltd
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    protein structures predicted by alphafold  (Deepmind Technologies Ltd)
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    CbbM_base: S162P, G422R, C6: H127V, M140A, K247A, H251A, Q392E, S432T + S162P, G422R, Ad1: H127V, K247A, H251A, Q392E, S432T, W114I + S162P, G422R. ( A ) Selectivity values of selected CbbM variants. (B ) Carboxylation rate constant ( k cat C ). ( C ) Oxygenation rate constant ( k cat O ). ( D ) Binding constant of CO2 in absence of oxygen, ( E ) of CO2 in air, ( F ) binding constant of O2. ( G ) Catalytic efficiency of carboxylation reaction in absence of air, ( H ) of carboxylation reaction in air, ( I ) catalytic efficiency of oxygenation reaction. All catalytic parameters were determined using a 14 CO2 fixation assay with four replicates. Statistical significance was assessed using a one-way ANOVA followed by Tukey’s multiple comparisons test ( J ) Visualization of important residues and active site in a CbbM model <t>(AlphaFold).</t> The dimers are shown in blue and yellow ( K ) Visualization of CbbM model displaying the location of residues mutated in variant Ad1. ( L ) Residue W114 (green) in CbbM constricts a tunnel (blue) in the dimer interface, connecting the two active sites.
    Protein Structures Predicted By Alphafold, supplied by Deepmind Technologies Ltd, 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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    protein structure predictions from alphafold  (Deepmind Technologies Ltd)
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    CbbM_base: S162P, G422R, C6: H127V, M140A, K247A, H251A, Q392E, S432T + S162P, G422R, Ad1: H127V, K247A, H251A, Q392E, S432T, W114I + S162P, G422R. ( A ) Selectivity values of selected CbbM variants. (B ) Carboxylation rate constant ( k cat C ). ( C ) Oxygenation rate constant ( k cat O ). ( D ) Binding constant of CO2 in absence of oxygen, ( E ) of CO2 in air, ( F ) binding constant of O2. ( G ) Catalytic efficiency of carboxylation reaction in absence of air, ( H ) of carboxylation reaction in air, ( I ) catalytic efficiency of oxygenation reaction. All catalytic parameters were determined using a 14 CO2 fixation assay with four replicates. Statistical significance was assessed using a one-way ANOVA followed by Tukey’s multiple comparisons test ( J ) Visualization of important residues and active site in a CbbM model <t>(AlphaFold).</t> The dimers are shown in blue and yellow ( K ) Visualization of CbbM model displaying the location of residues mutated in variant Ad1. ( L ) Residue W114 (green) in CbbM constricts a tunnel (blue) in the dimer interface, connecting the two active sites.
    Protein Structure Predictions From Alphafold, supplied by Deepmind Technologies Ltd, 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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    protein-structure-predicting ai alphafold  (Deepmind Technologies Ltd)
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    CbbM_base: S162P, G422R, C6: H127V, M140A, K247A, H251A, Q392E, S432T + S162P, G422R, Ad1: H127V, K247A, H251A, Q392E, S432T, W114I + S162P, G422R. ( A ) Selectivity values of selected CbbM variants. (B ) Carboxylation rate constant ( k cat C ). ( C ) Oxygenation rate constant ( k cat O ). ( D ) Binding constant of CO2 in absence of oxygen, ( E ) of CO2 in air, ( F ) binding constant of O2. ( G ) Catalytic efficiency of carboxylation reaction in absence of air, ( H ) of carboxylation reaction in air, ( I ) catalytic efficiency of oxygenation reaction. All catalytic parameters were determined using a 14 CO2 fixation assay with four replicates. Statistical significance was assessed using a one-way ANOVA followed by Tukey’s multiple comparisons test ( J ) Visualization of important residues and active site in a CbbM model <t>(AlphaFold).</t> The dimers are shown in blue and yellow ( K ) Visualization of CbbM model displaying the location of residues mutated in variant Ad1. ( L ) Residue W114 (green) in CbbM constricts a tunnel (blue) in the dimer interface, connecting the two active sites.
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    3-d protein structure prediction database alphafold  (Deepmind Technologies Ltd)
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    CbbM_base: S162P, G422R, C6: H127V, M140A, K247A, H251A, Q392E, S432T + S162P, G422R, Ad1: H127V, K247A, H251A, Q392E, S432T, W114I + S162P, G422R. ( A ) Selectivity values of selected CbbM variants. (B ) Carboxylation rate constant ( k cat C ). ( C ) Oxygenation rate constant ( k cat O ). ( D ) Binding constant of CO2 in absence of oxygen, ( E ) of CO2 in air, ( F ) binding constant of O2. ( G ) Catalytic efficiency of carboxylation reaction in absence of air, ( H ) of carboxylation reaction in air, ( I ) catalytic efficiency of oxygenation reaction. All catalytic parameters were determined using a 14 CO2 fixation assay with four replicates. Statistical significance was assessed using a one-way ANOVA followed by Tukey’s multiple comparisons test ( J ) Visualization of important residues and active site in a CbbM model <t>(AlphaFold).</t> The dimers are shown in blue and yellow ( K ) Visualization of CbbM model displaying the location of residues mutated in variant Ad1. ( L ) Residue W114 (green) in CbbM constricts a tunnel (blue) in the dimer interface, connecting the two active sites.
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    CbbM_base: S162P, G422R, C6: H127V, M140A, K247A, H251A, Q392E, S432T + S162P, G422R, Ad1: H127V, K247A, H251A, Q392E, S432T, W114I + S162P, G422R. ( A ) Selectivity values of selected CbbM variants. (B ) Carboxylation rate constant ( k cat C ). ( C ) Oxygenation rate constant ( k cat O ). ( D ) Binding constant of CO2 in absence of oxygen, ( E ) of CO2 in air, ( F ) binding constant of O2. ( G ) Catalytic efficiency of carboxylation reaction in absence of air, ( H ) of carboxylation reaction in air, ( I ) catalytic efficiency of oxygenation reaction. All catalytic parameters were determined using a 14 CO2 fixation assay with four replicates. Statistical significance was assessed using a one-way ANOVA followed by Tukey’s multiple comparisons test ( J ) Visualization of important residues and active site in a CbbM model (AlphaFold). The dimers are shown in blue and yellow ( K ) Visualization of CbbM model displaying the location of residues mutated in variant Ad1. ( L ) Residue W114 (green) in CbbM constricts a tunnel (blue) in the dimer interface, connecting the two active sites.

    Journal: bioRxiv

    Article Title: The fitness landscape of a Form II rubisco in a photosynthetic bacterium guides engineering of oxygen tolerance

    doi: 10.64898/2025.12.07.690893

    Figure Lengend Snippet: CbbM_base: S162P, G422R, C6: H127V, M140A, K247A, H251A, Q392E, S432T + S162P, G422R, Ad1: H127V, K247A, H251A, Q392E, S432T, W114I + S162P, G422R. ( A ) Selectivity values of selected CbbM variants. (B ) Carboxylation rate constant ( k cat C ). ( C ) Oxygenation rate constant ( k cat O ). ( D ) Binding constant of CO2 in absence of oxygen, ( E ) of CO2 in air, ( F ) binding constant of O2. ( G ) Catalytic efficiency of carboxylation reaction in absence of air, ( H ) of carboxylation reaction in air, ( I ) catalytic efficiency of oxygenation reaction. All catalytic parameters were determined using a 14 CO2 fixation assay with four replicates. Statistical significance was assessed using a one-way ANOVA followed by Tukey’s multiple comparisons test ( J ) Visualization of important residues and active site in a CbbM model (AlphaFold). The dimers are shown in blue and yellow ( K ) Visualization of CbbM model displaying the location of residues mutated in variant Ad1. ( L ) Residue W114 (green) in CbbM constricts a tunnel (blue) in the dimer interface, connecting the two active sites.

    Article Snippet: The structure of the designed variants used for tunnel analysis were predicted using the AlphaFold Protein Structure Database prediction server (DeepMind/EMBL-EBI) ( ).

    Techniques: Binding Assay, Variant Assay, Residue