Catálogo de publicaciones - revistas

<jats:title>Precise packing for membrane proteins</jats:title> <jats:p> Although nonpolar amino acid side chains pack efficiently in membrane proteins, it has been difficult to determine how much this contributes to membrane protein stability. Designed membrane proteins have largely relied on other stabilizing interactions such as metal-ligand interactions and hydrogen bonds. Mravic <jats:italic>et al.</jats:italic> uncovered a steric packing code underlying the folding of the natural protein phospholamban, which they used to design stable membrane proteins with nonpolar interfaces. They suggest that packing of nonpolar residues plays a role in the folding and stability of many membrane proteins. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6434" page="1418" related-article-type="in-this-issue" vol="363" xlink:href="10.1126/science.aav7541">1418</jats:related-article> </jats:p>

<jats:title>Threats to the Serengeti</jats:title> <jats:p> Protected areas are an important tool for conserving biodiversity and ecosystem functioning. But how well do these areas withstand pressure from human activity in surrounding landscapes? Veldhuis <jats:italic>et al.</jats:italic> studied long-term data from the Serengeti-Mara ecosystem in East Africa. Human activities at boundary regions cause animals to concentrate in the core of the protected area, which eventually reduces soil carbon storage and nitrogen fixation rates and increases vulnerability to extreme droughts. Similar patterns are likely for many, if not all, large protected areas. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6434" page="1424" related-article-type="in-this-issue" vol="363" xlink:href="10.1126/science.aav0564">1424</jats:related-article> </jats:p>