Amy E. Danson

ORCID: 0000-0003-0869-0459
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About
Contact & Profiles
Research Areas
  • Enzyme Structure and Function
  • Reproductive tract infections research
  • Protein Structure and Dynamics
  • Protein purification and stability
  • Immune Response and Inflammation
  • Bacterial Genetics and Biotechnology
  • Urinary Tract Infections Management
  • Mass Spectrometry Techniques and Applications
  • Brucella: diagnosis, epidemiology, treatment
  • Monoclonal and Polyclonal Antibodies Research
  • RNA and protein synthesis mechanisms
  • Bacteriophages and microbial interactions
  • Antibiotic Resistance in Bacteria
  • Advanced Biosensing Techniques and Applications
  • HIV Research and Treatment

National Physical Laboratory
2022-2023

University of Reading
2017-2020

Diamond Light Source
2020

Research Complex at Harwell
2020

Imperial College London
2019-2020

Computational design of protein-binding proteins is a fundamental capability with broad utility in biomedical research and biotechnology. Recent methods have made strides against some target proteins, but on-demand creation high-affinity binders without multiple rounds experimental testing remains an unsolved challenge. This technical report introduces AlphaProteo, family machine learning models for protein design, details its performance on the de novo binder problem. With we achieve 3- to...

10.48550/arxiv.2409.08022 preprint EN arXiv (Cornell University) 2024-09-12

Structure-function relationships of biological macromolecules, in particular proteins, provide crucial insights for fundamental biochemistry, medical research and early drug discovery. However, production recombinant either structure determination, functional studies, or to be used as biopharmaceutical products, is often hampered by their instability propensity aggregate solution vitro. Protein samples poor quality are associated with reduced reproducibility well high expenses. Several...

10.3389/fmolb.2022.890862 article EN cc-by Frontiers in Molecular Biosciences 2022-05-16

Chlamydia pneumoniae is a Gram-negative bacterium responsible for number of human respiratory diseases and linked to some chronic inflammatory diseases. The major outer membrane protein (MOMP) conserved immunologically dominant located in the membrane, which, together with its surface exposure abundance, has led MOMP being main focus vaccine antimicrobial studies recent decades. role chlamydial complex through formation intermolecular disulphide bonds, although exact interactions formed are...

10.3390/biology9100344 article EN cc-by Biology 2020-10-20

The major outer membrane protein (MOMP) from Chlamydophila pneumoniae is a promising candidate antigen for chlamydophila vaccine development. MOMP 40kDa protein, encoded by the gene omp1, accountable 60% of total mass pneumoniae. 2-3% all Gram negative genomes encode this particular class (porins), emphasising its importance and fueling intensive research into MOMPs structure function. Our interest in established link between human infection, micro-organisms such as pneumoniae,...

10.1107/s2053273314084939 article EN Acta Crystallographica Section A Foundations and Advances 2014-08-05

Understanding the structure-function relationships of macromolecules, such as proteins, at molecular level is vital for biomedicine and modern drug discovery. To date, X-ray crystallography remains most successful method solving three-dimensional protein structures atomic resolution. With recent advances in serial crystallography, either using free electron lasers (XFELs) or synchrotron light sources, has progressed to next frontier, where ability acquire time-resolved data provides...

10.3791/64744-v article EN 2023-03-04

Understanding the structure-function relationships of macromolecules, such as proteins, at molecular level is vital for biomedicine and modern drug discovery. To date, X-ray crystallography remains most successful method solving three-dimensional protein structures atomic resolution. With recent advances in serial crystallography, either using free electron lasers (XFELs) or synchrotron light sources, has progressed to next frontier, where ability acquire time-resolved data provides...

10.3791/64744 article EN Journal of Visualized Experiments 2023-03-03

Major outer membrane proteins (MOMPs) are structurally and immunologically dominant in the Chlam ydia membrane.Both surface exposure abundance of MOMP suggests a possible role ydia-host interactions, highlighting as vaccine target.The proposed beta-barrel structure, derived from homology modelling with FadL E. coli [1], also indicates ligand transport.Due to large number cysteine residues within lack detectable peptidoglycan ydia, it is hypothesised that may have structural forming...

10.1107/s2053273317091835 article EN Acta Crystallographica Section A Foundations and Advances 2017-12-01
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