An overview of the application of Fourier transform infrared spectroscopy for the analysis of
the structure of proteins and protein–ligand recognition is given. The principle of the …

X-ray crystallography is generally thought of as exploring structure, not mechanism. The
essence of a chemical or biological mechanism is time-dependent change in structure, not …

We report picosecond time-resolved x-ray diffraction from the myoglobin (Mb) mutant in
which Leu29 is replaced by Phe (L29Fmutant). The frame-by-frame structural evolution …

The effects of mutagenesis on geminate and bimolecular O 2 rebinding to 90 mutants at 27
different positions were used to map pathways for ligand movement into and out of sperm …

A time-resolved Laue X-ray diffraction technique has been used to explore protein relaxation
and ligand migration at room temperature following photolysis of a single crystal of carbon …

Synthetic organic polymers are typically insoluble polycrystalline or amorphous products
rather than single crystals. Here we demonstrate that covalent polymer chains can achieve …

Myoglobin (Mb) is perhaps the most studied protein, experimentally and theoretically.
Despite the wealth of known details regarding the gas migration processes inside Mb, there …

The GABAA receptor is an important target for a variety of general anesthetics (Franks and
Lieb, 1994) and for benzodiazepines such as diazepam. Specific point mutations in the …

The mesoporous silica SBA-15, functionalised with propylthiol groups during synthesis and
rendered porous (mean pore diameter 51 Å) by extraction of surfactant template molecules …

Although conformational changes are essential for the function of proteins, little is known
about their structural dynamics at atomic level resolution. Myoglobin (Mb) is the paradigm to …