Chromatin immunoprecipitation (ChIP), or location analysis, is an antibody-based method for identifying the segments of DNA recognized by a particular transcription factor in a native chromatin environment.
G-matrix Fourier transform (GFT) NMR, a technique developed several years ago for rapid collection of nuclear magnetic resonance data, has been used to determine the structures of eight proteins in less than a month.1 "People usually work for many months for one structure. And even a year is not unusual," says coauthor Thomas Szyperski of the University of Buffalo. [see related story, page 36]The work demonstrates for the first time that GFT NMR works on a "real world" scale, meaning a protein c
are a hot topic these days.
data that's essential for mathematical modeling of biological pathways.
Adult nematode worms contain 959 somatic cells, and thanks to Nobel laureate John Sulston and colleagues, scientists know the lineage of every one of them.
Geneticists subject to late-night bouts of inspiration generally have to write down their good ideas.
Two independent groups have demonstrated a new method for purifying proteins that may offer a simpler, cheaper alternative to large-scale column purification.
The Bruker AXS Smart Breeze X-ray crystallography system is an instrument that lives up to its name, says Bruker spokesperson Susan Byram.
Brian Fisher, curator of entomology at the California Academy of Sciences, has such enthusiasm for ants, he can make you feel guilty over spraying the little devils in your kitchen.
An interdisciplinary team at Rensselaer Polytechnic Institute (RPI) in Troy, NY, has developed a computer program that uses protein structural information to predict how proteins separate on a chromatography column.1 "This is something that is usually done by trial and error, but in this case we've used information from the experiment to build a computer model that enables us to make that prediction," explains coauthor Curt Breneman, a computational chemist at RPI.The technique first takes exper