Insight into protein structure and protein–ligand recognition by Fourier transform infrared spectroscopy
C Jung - Journal of Molecular Recognition, 2000 - Wiley Online Library
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 …
the structure of proteins and protein–ligand recognition is given. The principle of the …
Time-resolved biochemical crystallography: a mechanistic perspective
K Moffat - Chemical reviews, 2001 - ACS Publications
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 …
essence of a chemical or biological mechanism is time-dependent change in structure, not …
Watching a protein as it functions with 150-ps time-resolved x-ray crystallography
F Schotte, M Lim, TA Jackson, AV Smirnov, J Soman… - Science, 2003 - science.org
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 …
which Leu29 is replaced by Phe (L29Fmutant). The frame-by-frame structural evolution …
A solution processible single-crystal porous organic polymer
BT Liu, SH Gong, XT Jiang, Y Zhang, R Wang… - Nature …, 2023 - nature.com
Synthetic organic polymers are typically insoluble polycrystalline or amorphous products
rather than single crystals. Here we demonstrate that covalent polymer chains can achieve …
rather than single crystals. Here we demonstrate that covalent polymer chains can achieve …
Map** the pathways for O2 entry into and exit from myoglobin
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 …
different positions were used to map pathways for ligand movement into and out of sperm …
Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction
V Šrajer, Z Ren, TY Teng, M Schmidt, T Ursby… - Biochemistry, 2001 - ACS Publications
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 …
and ligand migration at room temperature following photolysis of a single crystal of carbon …
[HTML][HTML] Imaging the migration pathways for O2, CO, NO, and Xe inside myoglobin
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 …
Despite the wealth of known details regarding the gas migration processes inside Mb, there …
[PDF][PDF] Evidence for a common binding cavity for three general anesthetics within the GABAA receptor
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 …
Lieb, 1994) and for benzodiazepines such as diazepam. Specific point mutations in the …
Size selective protein adsorption on thiol-functionalised SBA-15 mesoporous molecular sieve
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 …
rendered porous (mean pore diameter 51 Å) by extraction of surfactant template molecules …
Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography
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 …
about their structural dynamics at atomic level resolution. Myoglobin (Mb) is the paradigm to …