A5065347787- Protein Structure and Dynamics
- Vector-Borne Animal Diseases
- RNA and protein synthesis mechanisms
- Chemical Reactions and Isotopes
- Escherichia coli research studies
- Advanced NMR Techniques and Applications
- Hemoglobin structure and function
- T-cell and Retrovirus Studies
- Animal Disease Management and Epidemiology
- Bacterial Genetics and Biotechnology
University of Jyväskylä
2020-2022
Abstract Unidirectional coherence transfer is highly efficient in intrinsically disordered proteins (IDPs). Their elevated ps-ns timescale dynamics ensures long transverse (T 2 ) relaxation times allowing sophisticated pathway selection comparison to folded proteins. 1 H α -detection non-susceptibility chemical exchange with the solvent and enables shift assignment of consecutive proline residues, typically abundant IDPs. However, many IDPs undergo a disorder-to-order transition upon...
Class I SH3 domain-binding motifs generally comply with the consensus sequence [R/K]xØPxxP, hydrophobic residue Ø being proline or leucine. We have studied unusual = Ala-specificity of SNX9 by determining its complex structure a peptide present in eastern equine encephalitis virus (EEEV) nsP3. The revealed length and composition n-Src loop as important factors specificity. also compared affinities EEEV nsP3 peptide, mutants, cellular ligands to SH3. These data suggest that has evolved...
Abstract LEE-encoded effector EspF (EspF) is an protein part of enteropathogenic Escherichia coli ’s (EPEC’s) arsenal for intestinal infection. This intrinsically disordered contains three highly conserved repeats which together compose over half the protein’s complete amino acid sequence. EPEC uses to hijack host proteins in order promote In attack translocated, with other proteins, cell via type III secretion system. Inside stimulates actin polymerization by interacting Neural...