Over the past 30 years, atomic force microscopy (AFM) has played an important role in
elucidating the structure and properties of polymer surfaces. AFM-based techniques have …

Recent progress toward understanding the rheology of dilute solutions of flexible polymers
is reviewed, emphasizing experimental results from flows imaging single deoxyribonucleic …

Hydrophobic interactions guide protein folding, multidomain protein assembly, receptor–
ligand binding, membrane formation, and cellular transportation. On the macroscale …

Hydrophobicity underpins self-assembly in many natural and synthetic molecular and
nanoscale systems. A signature of hydrophobicity is its temperature dependence. The first …

The hydrophobic interaction is significantly responsible for driving protein folding and self-
assembly. To understand it, the thermodynamics, the role of water structure, the dewetting …

When a polymer molecule is subjected to a force (such as a tensile force) it responds and
this response gives information about the thermodynamics and structural properties of the …

Force induced globule-to-coil transitions have been studied in single homopolymer
(polystyrene) chains in water using atomic force microscopy-based force spectroscopy. The …

Field-driven transport through nanofluidic devices has emerged as one of the promising
tools for characterizing the conformational and dynamical response of long polyelectrolytes …

We investigate the behavior of a single chain condensate formed through polymer-assisted
condensation (PAC)[Sommer, J.-U.. Macromolecules 2022, 55, 4841–4851] under the …

The specific interactions of the pairs laminin binding protein (LBP)–purified tick‐borne
encephalitis viral surface protein E and certain recombinant fragments of this protein, as well …