LA JOLLA, CA — August 20, 2010 — ERepeatedly boosting brain levels of one natural painkiller soon shuts down the brain cell receptors that respond to it, so that the painkilling effect is lost, according to a surprising new study led by Scripps …
In what is a first for biology, a team of investigators is reporting that the human body makes ozone. The team has been slowly gathering evidence over the last few years that the human body produces the reactive gas — most famous as the ultraviolet ray-absorbing component of the ozone layer — as part of a mechanism to protect it from bacteria and fungi. “Ozone was a big surprise,” says researcher Bernard Babior. “But it seems that biological systems manufacture ozone, and that ozone has an effect on those biological systems.”
A group of scientists at The Scripps Research Institute have used algae to express an antibody that targets herpes virus, describing the work in an upcoming issue of the journal Proceedings of the National Academy of Sciences. This antibody could potentially be an ingredient in an anti-herpes topical cream or other anti- herpes treatments, but more importantly the algae expression technology that the TSRI team used could facilitate production of any number of human antibodies and other proteins on a massive scale.
From time immemorial, every living thing has shared the same basic set of building blocks — 20 amino acids from which all proteins are made. That is, until now: A group of scientists say they have, for the first time, created an organism that can produce a 21st amino acid and incorporate it into proteins completely on its own. The research should help probe some of the central questions of evolutionary theory. The project could eventually give concrete answers to questions that have generally been regarded as purely speculative: Is 20 the ideal number of basic building blocks? Would additional amino acids lead to organisms with enhanced function? Why has the genetic code not evolved further?
A group of scientists have used a powerful laser in combination with innovative quantum mechanical computations to measure the flexibility of mouse antibodies. The new technique, described in an upcoming issue of the journal Proceedings of the National Academy of Sciences, is significant because protein flexibility is believed to play an important role in antibody — antigen recognition, one of the fundamental events in the human immune system. “This is the first time anybody has ever gone into a protein and experimentally measured the frequency of vibrations in response to an applied force,” said Floyd Romesberg, assistant professor in the Department of Chemistry at The Scripps Research Institute, who led the study.