Size-dependent properties ofTl2Sestudied by NMR spectroscopy

Nanoparticle size determination by (1)H NMR spectroscopy.

High-resolution solution (1)H NMR spectroscopy has been used to characterize the size of Pd dendrimer-encapsulated nanoparticles (DENs). The Pd nanoparticles measured by this technique contain 55, 147, 200, or 250 atoms, and they are encapsulated within sixth-generation, hydroxyl-terminated poly(amidoamine) PAMAM dendrimers (G6-OH). Detailed analysis of the NMR data shows that signals arising f...

Unravelling Glycobiology by NMR Spectroscopy

Size-Dependent Spectroscopy of InP Quantum Dots

The spectroscopic behavior of colloidal InP quantum dots (QDs) has been investigated as a function of the mean QD diameter (which ranged from 26 to 60 Å). Absorption spectra show up to three peaks or shoulders which reflect excited state transitions in the QDs. Global photoluminescence (PL) spectra (excitation well to the blue of the absorption onset and which consequently excites most of the Q...

Extended para-hydrogenation monitored by NMR spectroscopy.

A system that provides a sustained hyperpolarized (1)H NMR signal in an aqueous medium is reported. The enhanced signal lasts much longer than typical (1)H T(1) values, uncovering new possibilities for implementing hyperpolarized (1)H NMR/MRI experiments or performing kinetics studies that would not otherwise be detectable.

Millisecond protein folding studied by NMR spectroscopy.

Proteins are involved in virtually every biological process and in order to function, it is necessary for these polypeptide chains to fold into the unique, native conformation. This folding process can take place rapidly. NMR line shape analyses and transverse relaxation measurements allow protein folding studies on a microsecond-to-millisecond time scale. Together with an overview of current a...