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Graphene is the two-dimensional form of carbon, a single layer of carbon atoms thought impossible as a free-standing crystal until created in 2004. Now researchers from the Department of Energy's Lawrence Berkeley National Laboratory and the University of California at San Diego, using Berkeley Lab's Advanced Light Source, have measured the extraordinary properties of graphene with an accuracy never before achieved, confirming many strange features but also revealing significant departures from theoretical predictions.

The protein XPD is one component of an essential repair mechanism that maintains the integrity of DNA. Pinpoint mutations of this single protein are responsible for three different human diseases associated with increased risk of cancer and accelerated aging: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy. Researchers at Lawrence Berkeley National Laboratory and the Scripps Research Institute have now solved the essential structure of XPD, revealing novel insights into the processes of aging and cancer.

The Hofmeister series governs the strengths of ions in inducing protein unfolding and many other phenomena and remains vital to protein chemistry to this day. Although it dates from the late 19th century, its mechanism has never been properly understood. A team led by Richard Saykally of DOE's Lawrence Berkeley National Laboratory has found strong experimental support for a new explanation of Hofmeister effects, known as the Law of Matching Water Affinities.

The pigment-binding protein CP29, one of the "minor" light-harvesting proteins in green plants, has been identified as a valve that permits or blocks the critical release of excess solar energy during photosynthesis. Furthermore, it has been proposed that the opening and closing of this valve can be controlled by raising or lowering ambient pH levels.