| Records |
Author  |
Frère, C.H.; Krützen, M.; Mann, J.; Connor, R.C.; Bejder, L.; Sherwin, W.B. |
| Title |
Social and genetic interactions drive fitness variation in a free-living dolphin population |
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Journal Article |
| Year |
2010 |
Publication |
Proc Natl Acad Sci USA |
Abbreviated Journal |
Proc. Natl. Acad. Sci. U.S.A. |
| Volume |
107 |
Issue |
46 |
Pages |
19949-19954 |
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| Abstract |
The evolutionary forces that drive fitness variation in species are of considerable interest. Despite this, the relative importance and interactions of genetic and social factors involved in the evolution of fitness traits in wild mammalian populations are largely unknown. To date, a few studies have demonstrated that fitness might be influenced by either social factors or genes in natural populations, but none have explored how the combined effect of social and genetic parameters might interact to influence fitness. Drawing from a long-term study of wild bottlenose dolphins in the eastern gulf of Shark Bay, Western Australia, we present a unique approach to understanding these interactions. Our study shows that female calving success depends on both genetic inheritance and social bonds. Moreover, we demonstrate that interactions between social and genetic factors also influence female fitness. Therefore, our study represents a major methodological advance, and provides critical insights into the interplay of genetic and social parameters of fitness. |
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Equine Behaviour @ team @ |
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6412 |
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| Author |
Griebenow, K.; Klibanov, A.M. |
| Title |
Lyophilization-induced reversible changes in the secondary structure of proteins |
Type |
Journal Article |
| Year |
1995 |
Publication |
Proc Natl Acad Sci USA |
Abbreviated Journal |
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| Volume |
92 |
Issue |
24 |
Pages |
10969-10976 |
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| Abstract |
Changes in the secondary structure of some dozen different proteins upon lyophilization of their aqueous solutions have been investigated by means of Fourier-transform infrared spectroscopy in the amide III band region. Dehydration markedly (but reversibly) alters the secondary structure of all the proteins studied, as revealed by both the quantitative analysis of the second derivative spectra and the Gaussian curve fitting of the original infrared spectra. Lyophilization substantially increases the beta-sheet content and lowers the alpha-helix content of all proteins. In all but one case, proteins become more ordered upon lyophilization. |
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Equine Behaviour @ team @ |
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6519 |
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