Printed ink on a coated aluminum sample was analyzed using a specular reflection accessory with the unique capability of simultaneous sample viewing.
This application note shows how LECO’s GDS instruments are ideal for investigating PVD coatings and the factors that determine their protection of substrate.
A novel mass spectrometry-based flavonoid profiling workflow is applied to characterize and structurally annotate a large number of unknown flavonoids in fruit juice and vegetable juice samples.
A newly developed high-throughput method for the quantitation of vitamin D using both multiplexed LC and on-line SPE is discussed.
A compact, MEMS-based, single-photodetector NIR device, the NanoQuest, is used to distinguish different types of textiles.
This study explores the use of a novel SERS substrate that can enhance the Raman signals of explosives that are present in picogram quantities in neat solutions using a visible laser wavelength and a compact Raman instrument.
The in situ combination of rheometry and Raman spectroscopy allows for real-time, synchronized measurement of both physical and chemical material properties.
The hyphenation of rheology and Raman spectroscopy enabled a more holistic depiction of the crystallization process and provided unique insights into the formation of cocoa butter polymorph form IV.
A procedure was developed to calibrate the wavenumber (energy shift) axis in Raman spectrometers, and it was tested in both portable and laboratory-based instruments.
A procedure was developed to calibrate the wavenumber (energy shift) axis in Raman spectrometers, and it was tested in both portable and laboratory-based instruments.
A procedure was developed to calibrate the wavenumber (energy shift) axis in Raman spectrometers, and it was tested in both portable and laboratory-based instruments.
A procedure was developed to calibrate the wavenumber (energy shift) axis in Raman spectrometers, and it was tested in both portable and laboratory-based instruments.
The TacticID-1064 ST has dedicated software and hardware designed to measure materials through both transparent and opaque containers. These through-barrier measurements remove the need for active sampling of potentially dangerous compounds such as fentanyl, leading to safer operations and reduced wait time for clear results. The 1064 nm laser is also an advantage for analyzing fluorescent or impure material. A Raman system with a 785 or 830 nm laser may generate fluorescence from these samples, which can overwhelm the Raman signal and make identification impossible. In this application note, we explore some of the capabilities of the TacticID-1064 ST.
In this study, a glycerol-fed, lab-scale E. coli bioprocess producing representative pharmaceutical compounds was monitored offline with a portable, high-sensitivity Raman spectrometer.
Interference from background fluorescence is a common challenge in Raman analysis. A study of three different types of biological samples was made to compare the ability of 785-nm and 1064-nm excitation to deal with this problem.
Interference from background fluorescence is a common challenge in Raman analysis. A study of three different types of biological samples was made to compare the ability of 785-nm and 1064-nm excitation to deal with this problem.
This method, for the evaluation of the enantiomeric purity of particular phosphonate derivatives, offers advantages in terms of cost, simplicity, and measurement speed.
This method, for the evaluation of the enantiomeric purity of particular phosphonate derivatives, offers advantages in terms of cost, simplicity, and measurement speed.
This method, for the evaluation of the enantiomeric purity of particular phosphonate derivatives, offers advantages in terms of cost, simplicity, and measurement speed.
This method, for the evaluation of the enantiomeric purity of particular phosphonate derivatives, offers advantages in terms of cost, simplicity, and measurement speed.
Dr Adam J. Hopkins, Metrohm, highlights the capabilities of the OMNIS near-infrared technology platform for more efficient and advanced sampling of liquids and solids.
The structural complexity of monoclonal antibodies (mAbs) challenges the capabilities of even the most advanced chromatography and mass spectrometry techniques. This study examines the use of micro-pillar array columns in combination with mass spectrometry for peptide mapping of both mAbs and antibody–drug conjugates (ADCs).
The structural complexity of monoclonal antibodies (mAbs) challenges the capabilities of even the most advanced chromatography and mass spectrometry techniques. This study examines the use of micro-pillar array columns in combination with mass spectrometry for peptide mapping of both mAbs and antibody–drug conjugates (ADCs).
The structural complexity of monoclonal antibodies (mAbs) challenges the capabilities of even the most advanced chromatography and mass spectrometry techniques. This study examines the use of micro-pillar array columns in combination with mass spectrometry for peptide mapping of both mAbs and antibody–drug conjugates (ADCs).
The impact of speed of analysis and selectivity to the depth of coverage and accuracy of the analyses are discussed.
Selecting the correct wavelengths or isotopes and optimizing flame, furnace, or plasma conditions can seem a daunting task for a novice user, with a multitude of opportunities to introduce errors and generate poor quality data. While most elemental analysis instruments have intuitive operating software, they lack the intelligence to guide the operator through the early stages of method development and overcome associated problems along the way. This study describes an automated, intelligent approach to method development for trace element analysis using optical emission spectroscopy, and exemplifies this capability with a suite of real-world sample matrices.
Since glycans are responsible for bioactivity, solubility, immunogenicity, and clearance rate from circulation, it is vital to have a detailed map of glycans in therapeutic glycoproteins. Detailed glycoprotein structural analysis must be able to identify the peptide sequence where the glycans are attached as well as the structure of the glycan portion, including oligosaccharide sequence and glycosyl linkages. This article details methods for mass spectrometry experiments on both released glycans (“glycomics”), as well as on intact glycopeptides (“glycoproteomics”) using electron transfer dissociation, high-energy collision dissociation, and collisioninduced dissociation fragmentation pathways, which are needed to fully elucidate the structure of glycoproteins.