Researchers at Stanford University purified the proteasome from the malaria parasite and examined its activity against hundreds of
different peptide sequences using a novel method developed at the University of California, San Francisco.
Not exact matches
When strung together in a
sequence, amino acids create
peptides and proteins with
different 3D structures and, consequently,
different biological functions.
Naturally occurring
peptides can be composed of 20
different amino acids, so there is a great deal of possible variation in their
sequences.
We have a short time period, and so we do about a billion experiments at a time, where we can genetically engineer our viruses to express
different random
peptide sequences and we can, you know, [in] about a one microliter sample we can introduce about a billion
different viruses to a semiconductor wafer or an electrode and have them see if they can actually molecularly imprint it or try to do a chemical and physical map to it so that they can actually then have a template to grow that material.
«What's critical with this and what has never been done before is that a single
peptide sequence will work against the toxic versions of a number of
different amyloid proteins and
peptides, regardless of their amino acid
sequence or the normal 3 - D structures.»