A5079891811- Protein Structure and Dynamics
- Enzyme Structure and Function
- Glycosylation and Glycoproteins Research
- Monoclonal and Polyclonal Antibodies Research
- Genomics and Phylogenetic Studies
- Galectins and Cancer Biology
- Advanced Proteomics Techniques and Applications
- Machine Learning in Bioinformatics
- RNA and protein synthesis mechanisms
- Bioinformatics and Genomic Networks
Vrije Universiteit Brussel
2021-2024
Ghent University
2022-2024
VIB-VUB Center for Structural Biology
2021
Traditionally, our understanding of how proteins operate and evolution shapes them is based on two main data sources: the overall protein fold amino acid sequence. However, a significant part proteome shows highly dynamic and/or structurally ambiguous behavior, which cannot be correctly represented by traditional fixed set static coordinates. Representing such behaviors remains challenging necessarily involves complex interpretation conformational states, including probabilistic...
We provide integrated protein sequence-based predictions via https://bio2byte.be/b2btools/. The aim of our is to identify the biophysical behaviour or features proteins that are not readily captured by structural biology and/or molecular dynamics approaches. Upload a FASTA file text input sequence provides from DynaMine backbone and side-chain dynamics, conformational propensities, derived EFoldMine early folding, DisoMine disorder, Agmata β-sheet aggregation. These predictions, several...
Abstract α‐1 acid glycoprotein (AGP) is one of the most abundant plasma proteins. It fulfills two important functions: immunomodulation, and binding to various drugs receptors. These different functions are closely associated modulated via changes in glycosylation cancer missense mutations. From a structural point view, glycans alter local biophysical properties protein leading diverse ligand‐binding spectrum. However, can typically not be observed resolved X‐ray crystallography structure...
Abstract The advent of accurate methods to predict the fold proteins initiated by AlphaFold2 is rapidly changing our understanding and helping their design. However, these are mainly trained on protein structures determined with X-ray diffraction, where packed in crystals at often cryogenic temperatures. They can therefore only reliably cover well-folded parts that experience few, if any, conformational changes. Experimentally, solution nuclear magnetic resonance (NMR) experimental method...