Uplc peptide csh c18 nanoacquity column

A nanoAcquity UPLC (Waters Corporation, Milford, MA) connected to a Xevo Q-TOF (Waters Corporation, UK) was used for LC-ESI-MS experiments. Tryptic peptides were first trapped on an UPLC Symmetry C18 nanoAcquity trap column (5 μm, 180 μm × 20 mm, Water Corporation) and then separated on an UPLC Peptide CSH C18 nanoAcquity column (1.7 μm, 75 μm × 250 mm, Waters Corporation). For separation, we applied an optimized method and parameters that were previously reported.^{21 (link)}In silico tryptic digestions of rGH and prediction of fragment ions were performed with web based applications, Proteomics Toolkit (Institute of Systems Biology, Seattle, WA) and ProteinProspector 5.21.2 (The University of California, San Francisco, CA).

A nanoAcquity UPLC (Waters Corporation, Milford, MA) connected to a Xevo Q-TOF (Waters Corporation, UK) was used for LC-ESI-MS experiments. Tryptic peptides were first trapped on an UPLC Symmetry C18 nanoAcquity trap column (5 μm, 180 μm × 20mm, Water Corporation) and then separated on an UPLC Peptide CSH C18 nanoAcquity column (1.7 μm, 75 μm x 250 mm, Waters Corporation). For separation and analysis, we applied an optimized method and previously reported mass spectrometry parameters [2 (link), 29 (link)]. In silico tryptic digestions of rGH and prediction of fragment ions were performed with the web-based application, Proteomics Toolkit (Institute of Systems Biology, Seattle, WA) and ProteinProspector 5.21.2 (The University of California, San Francisco, CA).