Figure 1. The pipeline of Aggrescan3D 2.0 server.

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Presentation transcript:

Figure 1. The pipeline of Aggrescan3D 2.0 server. Unless provided in the caption above, the following copyright applies to the content of this slide: © The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com Nucleic Acids Res, gkz321, https://doi.org/10.1093/nar/gkz321 The content of this slide may be subject to copyright: please see the slide notes for details.

Figure 2. Aggregation propensity for different multimeric proteins, calculated in static or dynamic modes. (A) The ... Figure 2. Aggregation propensity for different multimeric proteins, calculated in static or dynamic modes. (A) The aggregation propensity of the static input structure relative to that of the 12 dynamic models is represented for homodimers, heterodimers, antibodies or the complete set. In the color scale, dark blue indicates the static structure being the most soluble (ranking 1) and dark red the static structure being the most aggregation-prone (ranking 13). (B) Monoclonal antibody bevacizumab Fab fragment (PDB: 1BJ1) ran on static (left) or dynamic (right) modes. Unless provided in the caption above, the following copyright applies to the content of this slide: © The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com Nucleic Acids Res, gkz321, https://doi.org/10.1093/nar/gkz321 The content of this slide may be subject to copyright: please see the slide notes for details.

Figure 3. A3D 2.0 as a tool for the in silico redesign of more stable and soluble proteins. A3D structures of original ... Figure 3. A3D 2.0 as a tool for the in silico redesign of more stable and soluble proteins. A3D structures of original GFP (left) (PDB: 2B3Q:A) and engineered GFP/KKK mutant (right) (PDB: 6FWW) coloured according to the A3D score. Mutations lowering aggregation propensity, while maintaining protein stability are encircled. The mutated variant was experimentally shown to be 2-fold more resistant against aggregation (19). Unless provided in the caption above, the following copyright applies to the content of this slide: © The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com Nucleic Acids Res, gkz321, https://doi.org/10.1093/nar/gkz321 The content of this slide may be subject to copyright: please see the slide notes for details.

Figure 4. Automated mutations for variable heavy (VH) segment of a human germline antibody. (A) A3D 2.0 automated ... Figure 4. Automated mutations for variable heavy (VH) segment of a human germline antibody. (A) A3D 2.0 automated mutations output (the residues at the three antibody CDRs were excluded from the screening). (B) The blue highlighted mutations in panel A were combined to render triple mutant engineered antibody. Structures of wild type (PDB: 5I19) and the mutant, as predicted by A3D 2.0. Solubilizing mutations are encircled. The engineered antibody variant was experimentally shown to be 3-fold more resistant against aggregation (19). Unless provided in the caption above, the following copyright applies to the content of this slide: © The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com Nucleic Acids Res, gkz321, https://doi.org/10.1093/nar/gkz321 The content of this slide may be subject to copyright: please see the slide notes for details.