Single-molecule force spectroscopy sheds light onto the free energy landscapes governing
protein folding and molecular recognition. Since only a single molecule or single molecular …

Force spectroscopy has developed into an indispensable tool for studying folding and
binding of proteins on a single molecule level in real time. Design of the pulling geometry …

Graphene offers promising advantages for biomedical applications. However, adoption of
graphene technology in biomedicine also poses important challenges in terms of …

Melatonin (MEL) is a pleiotropic indolamine that reaches multiple intracellular targets.
Among these, MEL binds to calmodulin (CaM) with high affinity. In presence of Ca2+, CaM …

Folding is a ubiquitous process that nature uses to control the conformations of its molecular
machines, allowing them to perform chemical and mechanical tasks. Over the years …

The recent revolution in optics and instrumentation has enabled the study of protein folding
using extremely low mechanical forces as the denaturant. This exciting development has led …

Combining atomic force microscopy and fluorescence resonance energy transfer
spectroscopy (AFM-FRET), we have developed a single-molecule AFM-FRET nanoscopy …

Enzymatic reactions and related protein conformational dynamics are complex and
inhomogeneous, playing crucial roles in biological functions. The relationship between …

The flexibility in the structure of calmodulin (CaM) allows its binding to over 300 target
proteins in the cell. To investigate the structure-function relationship of CaM, we combined …

Protein–ligand interactions are ubiquitous and play important roles in almost every
biological process. The direct elucidation of the thermodynamic, structural and functional …