Industrial

This note describes the characteristics and importance of protein phosphorylation, as well as the method of qualitative analysis of protein phosphorylation using HPLC-Chip electron transfer dissociation ion trap mass spectrometry technology. By comparing the differences between collision-induced dissociation (CID) and electron transfer dissociation (ETD) mass spectrometry techniques, it demonstrates the ability to analyze samples using both CID and ETD in the same LC/MS run. Examples of the identification of site-specific phosphorylation using an Agilent HPLC-Chip system are provided.

This Application Note demonstrates how Intelligent Sample Loading automates and optimizes sample enrichment on the HPLC-Chip, and also shows how Intelligent Sample Loading increases the number of peptides detected in a protein digest test mixture.

This article introduces several label-free methods for the relative quantitation of proteins. These methods include comparing the mean peak area of all peptides identified for a protein in each sample, the peak area of a peptide found in both samples, the number of identified peptides in each sample, and the number of spectral hits in each sample.

This application note describes how to use the Agilent 1200 Series Rapid Resolution LC system and Agilent ZORBAX Rapid Resolution High Throughput columns to separate compounds in complex samples, how to calculate the empirical formula of unknown compounds from high mass accuracy data acquired with the Agilent 6210 time-of-flight and teh Agilent 6510 Q-TOF mass spectrometer, how to use the Agilent MassHunter Profiling software to quickly and computer-assistedly analyze complex mass spectrometry data, and how to use the Agilent MassHunter Profiling software to analyze the differences in related samples in different applications.

This Application Note describes the quantitative analysis of carbohydrates in fruit juices. The analysis technique deployed the Agilent 1200 Series evaporative light scattering detector, which proved to be a viable alternative to refractive index detection because of lower susceptibility to temperature fluctuations and the possibility to perform gradient analyses. Correlation coefficients greater than 0.99 were achieved for the carbohydrates glucose, fructose, sucrose and sorbitol.

An LC/MS method was developed to monitor several coumarin rodenticides in complex matrices.

This application describes a method for analyzing intact triglycerides by LC/MS and the type of information available.

Four commercial natural colorants – red cabbage, Monascus, paprika, and lac – were analyzed using ESI and APCI-LC/MS. The MS data provided molecular weight information and some structural information for the major components in these pigments.

This document describes an alternative to 2D gel electrophoresis based on isoelectric point OFFGEL electrophoresis and high-sensitivity on-chip protein detection using the Agilent 2100 bioanalyzer.

This article discusses the use of atomic force microscopy (AFM) to probe the three-dimensional structure of soft organized surfactants at the solid-liquid interface. By utilizing Agilent Technologies' MAC Mode, precise control of the oscillation of a magnetically coated AFM cantilever is achieved, enabling imaging with an average force below 1 pN and minimizing distortion of soft molecules.

This document describes the application of Agilent 5500 or 5100 MAC Mode AFM for studying zinc-induced DNA kinking. It highlights the significance of DNA bending and the advantages of AFM in detecting structural fluctuations in DNA.

This article describes the application of scanning probe studies on a metalloprotein, with a focus on the analysis and control of biological oxidases, as well as the generation of biosensing systems targeting specific compounds.

This article introduces the evolution of scanning probe microscopes in biological imaging