
A multilaboratory collaborative study organized by the Human Proteome Organization demonstrated that participating laboratories had difficulty in identifying components of a simple protein mixture.
Tim Wehr is staff scientist at Bio-Rad Laboratories, Hercules, California. Direct correspondence about this column to Direct correspondence about this column to "Directions in Discovery," LCGC, Woodbridge Corporate Plaza, 485 Route 1 South, Building F, First Floor, Iselin, NJ 08830, e-mail lcgcedit@lcgcmag.com.

A multilaboratory collaborative study organized by the Human Proteome Organization demonstrated that participating laboratories had difficulty in identifying components of a simple protein mixture.

Following the sequencing of the human genome, the biological science community has moved to tackle the human proteome.

ERLIC is a new technique that shows promise as an alternative or complementary technique for both enrichment and separation of these posttranslationally-modified peptides.

A number of commercial in-solution, and in-gel IEF fractionation systems are described in this month's column.

This installment of "Directions in Discovery" will review current phosphorylation enrichment techniques with a focus on new developments.

In the last year, two new protein depletion products have been introduced, and these will be the focus of this month's installment of "Directions in Discovery."

Quantitative assessment of protein expression in biological systems in response to perturbations is an important element in the discovery and validation of biomarkers and drug targets. This can be a challenging task given the complexity and dynamic range of biological extracts. Many methods are currently in use to address protein quantification. This installment of "Directions in Discovery" reviews several of the more popular ones and reports on a collaborative study organized by the Association of Biomolecular Resource Facilities.

September 2006. Top-down and bottom-up are alternative strategies for protein identification and characterization by mass spectrometry. How do they fit into the world of proteomics? What are their implications for separation technology? These questions are addressed in this installment of "Directions in Discovery."

This is the second installment of a two-part series on the practical aspects of configuring and operating a nano liquid chromatography-mass spectrometry (LC-MS) system.

The first of a two-part series addresses HPLC pumps, sample introduction systems, and columns for nanoLC-MS.


Almost 40 years have passed since the concept of capillary electrophoresis (CE) was described by Hjertén (1) in 1967. It emerged as a viable analytical technique after the pioneering work of Jorgenson (2) in the early 1980s, and commercial instruments were first introduced at the end of that decade. It is appropriate at this time to survey the history of CE and to judge its success in the world of analytical instrumentation.

In this month's installment of "Directions in Discovery," the authors discuss how, with the arrival of combinatorial libraries and high-throughput screening, pharmaceutical firms can develop new models of drug discovery that not only lessen the initial capital outlay involved in drug discovery, but also refine the discovery process.

This month's "Directions in Discovery" looks at column and mobile-phase selection as well as system components and modification. Making the right choices among these parameters will help analysts get the most out of their liquid chromatography–mass spectrometry systems.

In this first installment of this new column, editor Tim Wehr explores the evolution of drug discovery and the analytical challenges that lie ahead.

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