Wignerian symplectic covariance approach to the interaction-time problem.

The concept of the symplectic covariance property of the Wigner distribution function and the symplectic invariance of the Wigner-Rényi entropies has been leveraged to estimate the interaction time of the moving quantum state in the presence of an absolutely integrable time-dependent potential. For this study, the considered scattering centre is represented initially by the Gaussian barrier. Two modifications of this potential energy are considered: a sudden change from barrier to barrier and from barrier to well.

Thermostable phenylacetic acid degradation protein TtPaaI from Thermus thermophilus as a scaffold for tetravalent display of proteins.

Numerous proteins in nature strictly require oligomerization for their full activity. Moreover, the function of natural and artificial proteins can me adjusted by altering their oligomeric state, leading to development of biotechnologically-relevant biomacromolecules. Oligomerization scaffolds from natural sources and designed de novo enable shuffling the oligomeric state and valency of biomacromolecules.

Engineered intrinsically fluorescent galectin-8 variants with altered valency, ligand recognition and biological activity.

Galectin-8 is a small soluble lectin with two carbohydrate recognition domains (CRDs). N- and C-terminal CRDs of Gal-8 differ in their specificity for glycan ligands. Here, we wanted to find out whether oligomerization of individual CRDs of galectin-8 affects its biological activity.

The diverse dependence of galectin-1 and -8 on multivalency for the modulation of FGFR1 endocytosis.

Fibroblast growth factor receptor 1 (FGFR1) is a N-glycosylated cell surface receptor tyrosine kinase, which upon recognition of specific extracellular ligands, fibroblast growth factors (FGFs), initiates an intracellular signaling. FGFR1 signaling ensures homeostasis of cells by fine-tuning essential cellular processes, like differentiation, division, motility and death. FGFR1 activity is coordinated at multiple steps and unbalanced FGFR1 signaling contributes to developmental diseases and cancers.