Structural dynamics inside a functionalized metal-organic framework probed by ultrafast 2D IR spectroscopy.

Structural Dynamics at Monolayer−Liquid Interfaces Probed by 2D IR Spectroscopy

Monolayers functionalized with tricarbonyl1,10-phenanthroline rhenium chloride (RePhen(CO)3Cl) are studied in the presence of a variety of polar organic solvents (chloroform, tetrahydrofuran, dimethylformamide, acetonitrile), hexadecane, and water. The headgroup, RePhen(CO)3Cl, is soluble in the bulk polar organic solvents but not in hexadecane or water. The surface structural dynamics are stud...

Structural dynamics of a catalytic monolayer probed by ultrafast 2D IR vibrational echoes.

Ultrafast two-dimensional infrared (2D IR) vibrational echo spectroscopy has proven broadly useful for studying molecular dynamics in solutions. Here, we extend the technique to probing the interfacial dynamics and structure of a silica surface-tethered transition metal carbonyl complex--tricarbonyl (1,10-phenanthroline)rhenium chloride--of interest as a photoreduction catalyst. We interpret th...

In this paper, the effect of nanocatalytic metal-organic framework based on copper metal and bis-tetrazolamine (CuBTA) ligand functionalized with cobalt (II) oxide nanoparticles on the thermal decomposition behavior of ammonium perchlorate (AP), using differential survey calorimetry (DSC) has been reviewed. First, the metal-organic framework (CuBTA) was synthesized from the raw materials of cop...

Transient two-dimensional infrared spectroscopy – towards measuring ultrafast structural dynamics

Ultrafast two-dimensional infrared spectroscopy (2D-IR) is a promising tool for the investigation of molecular structures [1-3] and their equilibrium fluctuations [2, 4]. Similar to 2D-NMR spectroscopy [5], cross-peaks between coupled states emerge in 2D-IR spectra, and contain structural information [2, 6]. The outstanding feature of 2D-IR spectroscopy is the combination of its structure resol...

Disulfide bond influence on protein structural dynamics probed with 2D-IR vibrational echo spectroscopy.

Intramolecular disulfide bonds are understood to play a role in regulating protein stability and activity. Because disulfide bonds covalently link different components of a protein, they influence protein structure. However, the effects of disulfide bonds on fast (subpicosecond to approximately 100 ps) protein equilibrium structural fluctuations have not been characterized experimentally. Here,...