The aggregation of proteins is of fundamental relevance in a number of daily phenomena,
as important and diverse as blood coagulation, medical diseases, or cooking an egg in the …

Although the kinetics and mechanisms of electron transfer reactions in homogeneous
solution have been intensively studied by the inorganic reaction mechanisms community …

Time-resolved fluorescence spectroscopy is used increasingly to probe molecular motions
at the aqueous interfaces of biological macromolecules and membranes. By recording the …

The quasi-bound biological or structuredwater molecules in a protein play a key role in
many biological processes. The dynamics of the biological water has been studied by …

The heterogeneous nature of a protein surface plays an essential role in its biological
activity and molecular recognition, and this role is mediated at least partly through the …

The time-dependent fluorescence frequency shift of protein-attached probes has a much
slower decay than that for the free probe. The decay times, ranging from 10 ps to several …

Over the past 20 years, the most studied and debated aspect of macromolecular crowding is
how it affects protein stability. Traditionally, it is explained by a delicate balance between the …

The mechanism of protein stabilization by osmolytes remains one of the most important and
long-standing puzzles. The traditional explanation of osmolyte-induced stability through the …

Fluorescence anisotropy decay and solvation dynamics of coumarin 153 (C153) are studied
in dimethyl β-cyclodextrin (DIMEB) and trimethyl β-cyclodextrin (TRIMEB) nanocavity in …

A biomolecular chromophore can be viewed as a quantum system with a small number of
degrees of freedom interacting with an environment (the surrounding protein and solvent) …