Landscape-Scale Implications of the Edge Effect on Soil Fauna Activity in a Temperate Forest

Although studies on edge effects on species richness and abundance are numerous, the responses of ecosystem processes to these effects have received considerably less attention. How ecosystem processes respond to edge effects is particularly important in temperate forests, where small fragments and edge habitats form a considerable proportion of the total forest area. Soil fauna are key contributors to decomposition and soil biogeochemical cycling processes. Using the bait lamina technique, we quantified soil fauna feeding activity, and its dependence on soil moisture and distance to the edge in a broad-leaved forest in Southern England. Feeding activity was 40% lower at the forest edge than in the interior, and the depth of edge influence was approximately 75 m. A watering treatment showed that moisture limitation was the main driver of the reduced feeding activity at the edge. In England, only 33% of the forest area is greater than 75 m from the edge. Therefore, assuming that the results from this single-site study are representative for the landscape, it implies that only one- third of the forest area in England supports activity levels typical for the forest core, and that edge effects reduce the mean feeding activity across the landscape by 17% (with lower and upper 90% confidence intervals of 1.3 and 23%, respectively). Changing climatic conditions, such as summer droughts may exacerbate such effects as edges lose water faster than the forest interior. The results highlight the importance of taking edge effects into account in ecological studies and forest management planning in highly fragmented landscapes.Peer reviewe

Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy

The atomic resolution structure of fd coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles differs from that previously determined by x-ray fiber diffraction. Most notably, the 50-residue protein is not a single curved helix, but rather is a nearly ideal straight helix between residues 7 and 38, where there is a distinct kink, and then a straight helix with a different orientation between residues 39 and 49. Residues 1–5 have been shown to be mobile and unstructured, and proline 6 terminates the helix. The structure of the coat protein in virus particles, in combination with the structure of the membrane-bound form of the same protein in bilayers, also recently determined by solid-state NMR spectroscopy, provides insight into the viral assembly process. In addition to their roles in molecular biology and biotechnology, the filamentous bacteriophages continue to serve as model systems for the development of experimental methods for determining the structures of proteins in biological supramolecular assemblies. New NMR results include the complete sequential assignment of the two-dimensional polarization inversion spin-exchange at the magic angle spectrum of a uniformly (15)N-labeled 50-residue protein in a 1.6 × 10(7) Da particle in solution, and the calculation of the three-dimensional structure of the protein from orientational restraints with an accuracy equivalent to an rms deviation of ≈1Å