Scanning electron micrographs of silica colloidal crystals on the same size scale for (A) 490 ± 10 nm particles and (B) 145 ± 3 nm particles. Department of Chemistry Published in: Angela R. Soemo; Mary J. Wirth; Langmuir 2010, 26, 2196-2199. DOI: 10.1021/la9038914 Copyright 2010 American Chemical Society
Images of a silica colloidal crystal packed in a capillary. Photographs through an optical microscope for (a) end-on view and (b) side-on view. (c) SEM image of the end-on view of a region of the capillary. Department of Chemistry Published in: Douglas S. Malkin; Bingchuan Wei; Arthur J. Fogiel; Sau Lan Staats; Mary J. Wirth; Anal. Chem. Article ASAP DOI: 10.1021/ac100062t Copyright 2010 American Chemical Society
Raw electrochromatograms for DiI-C12 at four different electric fields, superimposed on the same time axis, without removing the contribution from injected width. The mobile phase was 90:10 MeOH/water and 0.1% formic acid, and the stationary phase was horizontally polymerized C18/C1. Department of Chemistry Published in: Douglas S. Malkin; Bingchuan Wei; Arthur J. Fogiel; Sau Lan Staats; Mary J. Wirth; Anal. Chem. Article ASAP DOI: 10.1021/ac100062t Copyright 2010 American Chemical Society
Plot of plate height (corrected for injected width) vs analyte migration rate. The circles are experimental data, and the solid curve is H = 2γD/v. Regression showed that A = 0 ± 20 nm. Department of Chemistry Published in: Douglas S. Malkin; Bingchuan Wei; Arthur J. Fogiel; Sau Lan Staats; Mary J. Wirth; Anal. Chem. Article ASAP DOI: 10.1021/ac100062t Copyright 2010 American Chemical Society
LC-MS/MS analyses of E. coli cell lysate using the 15 cm long silica particle-packed column and the 350 cm long monolithic silica column. The results obtained with the 15 cm long, 3 μm C18 silica particle-packed column (triangles) and the 350 cm monolithic silica column (circles) are shown. Injected amounts are indicated in parentheses. (A) The number of identified peptides, (B) the average W1/2 values of 9 commonly identified peptides, and (C) the peak capacity are indicated. The mobile phases consisted of (A) 0.5% acetic acid and (B) 0.5% acetic acid and 80% acetonitrile. A two-step linear gradient of 5 40% B delivered over a variable time (70 2470 min), followed by 40 100% B in 5 min, and 100% B for 10 min was employed. The column pressure at t0 was 11.8 and 17.3 MPa for the particle-packed column (t0 = 6.7 min) and the monolithic silica column (t0 = 79.9 min), respectively. Department of Chemistry Published in: Mio Iwasaki;
Base peak chromatograms for the analysis of E. coli cell lysate using the 15 cm long C18 silica particle-packed column (A) and the 350 cm long monolithic silica C18 column (B). Tryptic peptides in 4 μg of E. coli cell lysate were loaded onto each column. Gradients of 70 and 2470 min were applied to the 15 cm long particle-packed column and the 350 cm long monolithic silica column, respectively. Other conditions are described in Figure 1. Department of Chemistry Published in: Mio Iwasaki; Shohei Miwa; Tohru Ikegami; Masaru Tomita; Nobuo Tanaka; Yasushi Ishihama; Anal. Chem. Article ASAP DOI: 10.1021/ac100343q Copyright 2010 American Chemical Society
Comparison of peak responses obtained by LC-MSMS using the 15 cm long particle-packed column with those using the 350 cm long monolithic silica column. (A) Peak responses of 1458 peptides identified commonly by the use of the 15 cm long particle-packed column and the 350 cm long monolithic silica column are plotted. The response was measured by integrating the peak area in the XIC chromatogram of the corresponding peptide. (B) XIC chromatogram (upper panel) and MS spectrum (bottom panel) of a doubly charged peptide of m/z 618.28, EGQNLDFVGGAE, from 50S ribosomal subunit protein L23 (JW3280). The 15 cm long particle-packed column was used. The MS spectrum was collected at the peak top in the XIC chromatogram. Other conditions are described in Figure 2. (C) XIC chromatogram (upper panel) and MS spectrum (bottom panel) of the same peptide as in (B). The 350 cm long monolithic silica column was used. Department of Chemistry Published in: Mio Iwasaki; Shohei Miwa; Tohru Ikegami; Masaru Tomita; Nobuo Tanaka; Yasushi Ishihama; Anal. Chem. Article ASAP DOI: 10.1021/ac100343q Copyright 2010 American Chemical Society
SEM images of (a) the SiO2 template together with the novel TiO2 replica (b) spheres used in the enrichment protocol. Department of Chemistry Published in: Alexander Leitner; Martin Sturm; Otto Hudecz; Michael Mazanek; Jan-Henrik Sma tt; Mika Lindén; Wolfgang Lindner; Karl Mechtler; Anal. Chem. Article ASAP Copyright 2010 American Chemical Society
Analytical strategy for the enrichment of HeLa phosphopeptides by metal oxide affinity chromatography. Department of Chemistry Published in: Alexander Leitner; Martin Sturm; Otto Hudecz; Michael Mazanek; Jan-Henrik Sma tt; Mika Lindén; Wolfgang Lindner; Karl Mechtler; Anal. Chem. Article ASAP Copyright 2010 American Chemical Society
Comparison of phosphopeptides identified by the three metal oxide materials. (a) Total number of phosphopeptides identified (in at least one of three replicates) and (b) distribution according to the number of phosphorylation sites per peptide. Department of Chemistry Published in: Alexander Leitner; Martin Sturm; Otto Hudecz; Michael Mazanek; Jan-Henrik Sma tt; Mika Lindén; Wolfgang Lindner; Karl Mechtler; Anal. Chem. Article ASAP Copyright 2010 American Chemical Society
Overlaps (in %) in the phosphopeptide identifications from the three metal oxide materials. (a) Overlap of phosphopeptide identifications in different technical replicates. (b) Overlap of phosphopeptides (identified at least in one of three replicates) for the three metal oxide materials. Department of Chemistry Published in: Alexander Leitner; Martin Sturm; Otto Hudecz; Michael Mazanek; Jan-Henrik Sma tt; Mika Lindén; Wolfgang Lindner; Karl Mechtler; Anal. Chem. Article ASAP Copyright 2010 American Chemical Society
Schematic diagram of the system with automated sample injection and isotope dimethyl labeling. Solid line: sample injection and sequential isotope dimethyl labeling onto the RP-SCX biphasic trap column; dashed line: stepwise salt eluting of sample to analytical column and gradient RPLC analysis. Published in: Fangjun Wang; Rui Chen; Jun Zhu; Deguang Sun; Chunxia Song; Yifeng Wu; Mingliang Ye; Liming Wang; Hanfa Zou; Anal. Chem. Article ASAP Department DOI: 10.1021/ac100075y of Chemistry Copyright 2010 American Chemical Society
Base peak chromatograms of an 11-cycle online multidimensional analysis of isotope dimethyl labeled samples (HCC liver sample labeled with light dimethyl groups and normal liver sample labeled with heavy dimethyl groups). The three buffer solutions used for the chromatography were 0.1% formic acid aqueous solution (buffer A), 0.1% formic acid ACN (buffer B), and 1000 mm ammonium acetate at ph 2.7 (buffer C). Cycle 1 (0 mm) consisted of a 5 min gradient from 0 to 10% buffer B, a 90 min gradient from 10 to 35% buffer B, and a 5 min gradient from 35 to 80% buffer B, after a 10 min hold at 80% buffer B, the system was equilibrated with 100% buffer A for 15 min. Each of the next nine cycles was 150 min with the follow procedures: 10 min of X% buffer C, 15 min of 100% buffer A, then the separation gradient was just the same as cycle 1. The 10 min buffer C in cycle 2-10 was as follows: cycle 2, 5% (50 mm); cycle 3, 10% (100 mm); cycle 4, 15% (150 mm); cycle 5, 20% (200 mm); cycle 6, 25% (250 mm); cycle 7, 30% (300 mm); cycle 8, 35% (350 mm); cycle 9, 40% (400 mm); cycle 10, 50% (500 mm). Cycle 11 (1000 mm) consisted of a 20 min 100% buffer C wash followed by a 15 min 100% buffer A wash, and the separation gradient was also the same as cycle 1. Department of Chemistry