<?xml version="1.0" encoding="utf-8"?>
<rss version="2.0" xml:base="http://harvardscience.harvard.edu" xmlns:dc="http://purl.org/dc/elements/1.1/">
<channel>
 <title>all Tucker Collins stories</title>
 <link>http://harvardscience.harvard.edu/stories/person/1683</link>
 <description>Stories and external links referencing a person (RSS)</description>
 <language>en</language>
<item>
 <title>Disparate proteins structurally identical</title>
 <link>http://harvardscience.harvard.edu/medicine-health/articles/disparate-proteins-structurally-identical</link>
 <description>&lt;!--paging_filter--&gt;&lt;p&gt;Gerhard Wagner, the Elkan Blout professor of biological chemistry and molecular pharmacology, and Tucker Collins, the S. Burt Wolbach professor of pathology at Harvard Medical School and Children&#039;s Hospital, made a crucial connection between two unrelated proteins.  They were studying a particular type of protein when a database search for proteins with similar structures turned up a fragment of the HIV-1 capsid protein.  Given the propensity for retroviral proteins to rapidly mutate, this conserved interface offers an attractive therapeutic target for two reasons. It may be less likely to mutate, and it may be essential for capsid dimerization, which, in turn, is essential for viral replication.&lt;/p&gt;
</description>
 <pubDate>Mon, 26 Mar 2007 05:36:40 -0400</pubDate>
 <dc:creator>70652986</dc:creator>
 <guid isPermaLink="false">3530 at http://harvardscience.harvard.edu</guid>
</item>
</channel>
</rss>
