An Expanded Conformation of an Antibody Fab Region by X-Ray Scattering, Molecular Dynamics and smFRET Identifies an Aggregation Mechanism.
- Submitting institution
-
University College London
- Unit of assessment
- 12 - Engineering
- Output identifier
- 12610
- Type
- D - Journal article
- DOI
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10.1016/j.jmb.2019.02.009
- Title of journal
- J Mol Biol
- Article number
- -
- First page
- 1409
- Volume
- 431
- Issue
- 7
- ISSN
- 1089-8638
- Open access status
- Compliant
- Month of publication
- February
- Year of publication
- 2019
- URL
-
-
- Supplementary information
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https://ars.els-cdn.com/content/image/1-s2.0-S0022283619300865-mmc1.docx
- Request cross-referral to
- -
- Output has been delayed by COVID-19
- No
- COVID-19 affected output statement
- -
- Forensic science
- No
- Criminology
- No
- Interdisciplinary
- Yes
- Number of additional authors
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6
- Research group(s)
-
-
- Proposed double-weighted
- No
- Reserve for an output with double weighting
- No
- Additional information
- Multi-disciplinary collaboration to combine experimental and computational simulation techniques for unprecedented elucidation of structural conformations critical to loss of potency in therapeutic proteins. Data enabled published computational engineering of therapeutic proteins (10.1021/acs.molpharmaceut.8b00186). Presented in keynotes at CASSS (San Francisco, 2019), and ESACT (UK, 2020). Led to appointment to Leukocare GmbH Scientific Advisory Board, and as External Research Reviewer of Danish Technical University, Department of Chemistry. Led to three new collaborations with Oxford, Loloya (Chicago), Instituto Butantan (Brazil), to formulate COVID-19 and Zika vaccines, and a £260k Medical Research Foundation Fellowship (https://www.medicalresearchfoundation.org.uk/projects/how-is-the-molecule-β2gpi-involved-in-antiphospholipid-syndrome) to elucidate a key protein structure in antiphospholipid syndrome.
- Author contribution statement
- -
- Non-English
- No
- English abstract
- -