Imagine controlling a computer with just your mind.

has upped the ante in microfluidics-based gel electrophoresis.

A team of researchers at the University of California, San Diego, has harnessed the body's ability to tweak antibody genes to drive protein evolution in the lab.

X-ray crystallography typically is used to capture static images of molecular structure.

Membrane proteins comprise the majority of drug targets.

In the world of gene-expression profiling, microarrays reign, but they are not without drawbacks.

Like Sting's omnipresent voyeur, specialized mechanisms in the cells of higher organisms carefully monitor oxygen intake.

Most biological microscopes delve deep into the cell, imaging optical slices that can be put together into a three-dimensional rendering of what lies beneath the cell membrane.

In the mid-1950s, Princeton University researcher Marvin Minsky sought a way to increase signal-to-noise when imaging central nervous system samples.

Scientists at the Pacific Northwest National Laboratory in Richland, Wash., have used an established technique to observe real-time interactions between single protein molecules for the first time.

ERK1/2 ACTIVATIONCourtesy of Biosource Internationalis plainly visible in heart tissue from an MHC-Rac1 transgenic mouse (right), compared with its normal counterpart (left). Green, pERK 1/2 (pTEpY185/187); blue, actin; red, nuclei.Protein phosphorylation is one of the most widely studied posttranslational modifications, with good reason. Many cellular signaling events rely on the addition or subtraction of phosphate groups (by kinases and phosphatases, respectively) to serine, threonine, and ty

UPS AND DOWNS OF TRANSCRIPTION:© 2002 Elsevier ScienceGenomic DNA is wrapped around histone octamers to provide nucleosomes that are further compacted in chromatin fibers. To up-regulate a gene (a), the activator binds to a specific sequence and recruits various cellular machines that permit RNA polymerase and its associated proteins to bind and transcribe. During transcriptional repression (b), the repressor binds to a specific DNA site and recruits protein complexes that modify the histon