Drought-induced shift of a forest–woodland ecotone: Rapid landscape response to climate variation

In coming decades, global climate changes are expected to produce large shifts in vegetation distributions at unprecedented rates. These shifts are expected to be most rapid and extreme at ecotones, the boundaries between ecosystems, particularly those in semiarid landscapes. However, current models do not adequately provide for such rapid effects—particularly those caused by mortality—largely because of the lack of data from field studies. Here we report the most rapid landscape-scale shift of a woody ecotone ever documented: in northern New Mexico in the 1950s, the ecotone between semiarid ponderosa pine forest and piñon–juniper woodland shifted extensively (2 km or more) and rapidly (<5 years) through mortality of ponderosa pines in response to a severe drought. This shift has persisted for 40 years. Forest patches within the shift zone became much more fragmented, and soil erosion greatly accelerated. The rapidity and the complex dynamics of the persistent shift point to the need to represent more accurately these dynamics, especially the mortality factor, in assessments of the effects of climate change.

Spectral diffusion and the energy landscape of a protein

We present a novel type of spectral diffusion experiment in the millikelvin range to characterize the energy landscape of a protein as compared with that of a glass. We measure the time evolution of spectral holes for more than 300 hr after well-defined initial nonequilibrium conditions. We show that the model of noninteracting two-level systems can describe spectral diffusion in the glass, but fails for the protein. Our results further demonstrate that randomness in the energy landscape of a protein shows features of organization. There are “deep minimum” states separated by barriers, the heights of which we are able to estimate. The energy landscape of a glass is featureless by comparison.

The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin

The grail of protein science is the connection between structure and function. For myoglobin (Mb) this goal is close. Described as only a passive dioxygen storage protein in texts, we argue here that Mb is actually an allosteric enzyme that can catalyze reactions among small molecules. Studies of the structural, spectroscopic, and kinetic properties of Mb lead to a model that relates structure, energy landscape, dynamics, and function. Mb functions as a miniature chemical reactor, concentrating and orienting diatomic molecules such as NO, CO, O2, and H2O2 in highly conserved internal cavities. Reactions can be controlled because Mb exists in distinct taxonomic substates with different catalytic properties and connectivities of internal cavities.