Gct premier high resolution time of flight mass spectrometer

Example 13

Materials and Methods:Unless stated otherwise, reactions were conducted under an atmosphere of N₂ using reagent grade solvents. DCM, and toluene were stored over 3 Å molecular sieves. THF was passed over a column of activated alumina. All commercially obtained reagents were used as received. Thin-layer chromatography (TLC) was conducted with E. Merck silica gel 60 F254 pre-coated plates (0.25 mm) and visualized by exposure to UV light (254 nm) or stained with p-anisaldehyde, ninhydrin, or potassium permanganate. Flash column chromatography was performed using normal phase silica gel (60 Å, 0.040-0.063 mm, Geduran). ¹H NMR spectra were recorded on Varian spectrometers (400, 500, or 600 MHz) and are reported relative to deuterated solvent signals. Data for ¹H NMR spectra are reported as follows: chemical shift (δ ppm), multiplicity, coupling constant (Hz) and integration. ¹³C NMR spectra were recorded on Varian spectrometers (100, 125, or 150 MHz). Data for ¹³C NMR spectra are reported in terms of chemical shift (δ ppm). Mass spectra were obtained from the UC Santa Barbara Mass Spectrometry Facility on a (Waters Corp.) GCT Premier high resolution time-of-flight mass spectrometer with a field desorption (FD) source.

Example 2

Crosslinkers and non-natural amino acids (NNAAs) were prepared based on the general design shown in FIG. 2.1.

Materials and Methods: Unless stated otherwise, reactions were conducted under an atmosphere of N₂ using reagent grade solvents. DCM, and toluene were stored over 3 Å molecular sieves. THF was passed over a column of activated alumina. All commercially obtained reagents were used as received. Thin-layer chromatography (TLC) was conducted with E. Merck silica gel 60 F254 pre-coated plates (0.25 mm) and visualized by exposure to UV light (254 nm) or stained with p-anisaldehyde, ninhydrin, or potassium permanganate. Flash column chromatography was performed using normal phase silica gel (60 Å, 0.040-0.063 mm, Geduran). ¹H NMR spectra were recorded on Varian spectrometers (400, 500, or 600 MHz) and are reported relative to deuterated solvent signals. Data for ¹H NMR spectra are reported as follows: chemical shift (6 ppm), multiplicity, coupling constant (Hz) and integration. ¹³C NMR spectra were recorded on Varian spectrometers (100, 125, or 150 MHz). Data for ¹³C NMR spectra are reported in terms of chemical shift (6 ppm). Mass spectra were obtained from the UC Santa Barbara Mass Spectrometry Facility on a (Waters Corp.) GCT Premier high-resolution time-of-flight mass spectrometer with a field desorption (FD) source.