Nature (Vol. 439, No. 7072, January 2006)

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From the Hardcover variation.

Additional resources for Nature (Vol. 439, No. 7072, January 2006)

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The declines occurred on a timescale equal to, or slightly less than, a single generation of these species. All of the species apart from N. chemnitzi also declined by 25–57% in mean size over the 17-year period (see supplementary information). The survey data are not adequate for full assessment of the situation for other deep-sea fish species that may also be at risk. 0 1975 1980 1985 Year 1990 1995 Figure 1 | Trends in relative abundance of five species of deep-sea fish. Weighted relative abundance (number per tow) over time from research-survey data, showing the estimated exponential decline (red line) and 95% confidence projections of the estimate (dashed lines) for five deep-sea species in the Canadian waters of the northwest Atlantic, 1978–94.

8. Haedrich, R. , Merrett, N. R. & O’Dea, N. R. Fish. Res. 51, 113–122 (2001). 9. Moore, J. A. & Mace, P. M. Fisheries 24, 22–23 (1999). Supplementary information accompanies this communication on Nature’s website. Competing financial interests: declared none. com/bca see Nature contents. 8 20 c 0 2,000 4,000 0 Frequency of different consumer and resource types 0 2,000 4,000 b a 0 A variety of mechanisms can theoretically produce competitive coexistence in nature1, making it hard to identify a single explanation for the maintenance of diversity in any particular system.

Subsequent refolding and assembly of HRA and HRB into a six-helix bundle (6HB) occurs, placing the fusion peptides and the transmembrane domains in proximity13,17. Formation of the 6HB and the associated free-energy change are tightly linked to merger of the viral and cellular membranes16,18. The isolated F 6HB structure, generated from HRA and HRB peptides17,19, is stable up to 100 8C and is thought to represent the lowest-energy conformation of the protein after membrane fusion. We previously reported the structure of the uncleaved, secreted hPIV3 F0 ectodomain (solF0), truncated before the transmembrane domain20.

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