Team:UCLA/HumanPractices

From 2013.igem.org

(Difference between revisions)
(Replaced content with "{{:Team:UCLA/Template}}")
Line 1: Line 1:
-
<html>
+
{{:Team:UCLA/Template}}
-
<head><link href='http://fonts.googleapis.com/css?family=Raleway' rel='stylesheet' type='text/css'>
+
-
<style type="text/css">
+
-
 
+
-
.bg {
+
-
  background: url('https://static.igem.org/mediawiki/2013/7/72/Bg_main2.jpg') repeat;
+
-
  position: fixed;
+
-
  width: 100%;
+
-
  height: 300%;
+
-
  top:0;
+
-
  left:0;
+
-
  z-index: -1;
+
-
}
+
-
section {
+
-
  color: black;
+
-
  font-family: 'Raleway', sans-serif;
+
-
  width: 750px;
+
-
  margin: auto;
+
-
  line-height: 20px;
+
-
  font-size: 16px;
+
-
}
+
-
outline { position: relative; height: 600px; width: 800px; margin: 18px auto 0; border: solid 1px #999; }
+
-
 
+
-
</style>
+
-
<script src="https://ajax.googleapis.com/ajax/libs/jquery/1.4.4/jquery.min.js"></script>
+
-
<script>
+
-
$(window).scroll(function(e){
+
-
  parallax();
+
-
});
+
-
function parallax(){
+
-
  var scrolled = $(window).scrollTop();
+
-
  $('.bg').css('top',-(scrolled*0.1)+'px');
+
-
}
+
-
</script>
+
-
</head>
+
-
<div class="bg"></div>
+
-
 
+
-
<section>
+
-
  <h1>UCLA iGEM</h1>
+
-
  <p>Both the mammalian immune system&#39;s complex defenses and a bacteriophage&#39;s targeting mechanism depend
+
-
upon protein diversification. These models have inspired innovations ranging from targeted drug delivery
+
-
to protein display. Using the major tropism determining (MTD) protein expressed on the Bordatella
+
-
bacteriophage BPP-1, we aim to develop an in vitro system for generating antibody-like proteins that
+
-
bind specified targets. The MTD protein expressed at the phage&#39;s tail fiber is naturally modified at
+
-
its variable region to produce nearly 10<sup>13</sup> possible binding variants while preserving its
+
-
structure. Mutating the MTD&#39;s variable region by PCR can match the massive diversity of MTD in vitro.
+
-
A library of MTD protein-DNA fusions generated by mRNA display can then be screened for binding
+
-
against specified protein targets. This in vitro analog to phage display and immune clonal selection
+
-
can be a powerful tool for constructing target-binding MTD variants with equally many varied applications.
+
-
</p> <p>Both the mammalian immune system&#39;s complex defenses and a bacteriophage&#39;s targeting mechanism depend
+
-
upon protein diversification. These models have inspired innovations ranging from targeted drug delivery
+
-
to protein display. Using the major tropism determining (MTD) protein expressed on the Bordatella
+
-
bacteriophage BPP-1, we aim to develop an in vitro system for generating antibody-like proteins that
+
-
bind specified targets. The MTD protein expressed at the phage&#39;s tail fiber is naturally modified at
+
-
its variable region to produce nearly 10<sup>13</sup> possible binding variants while preserving its
+
-
structure. Mutating the MTD&#39;s variable region by PCR can match the massive diversity of MTD in vitro.
+
-
A library of MTD protein-DNA fusions generated by mRNA display can then be screened for binding
+
-
against specified protein targets. This in vitro analog to phage display and immune clonal selection
+
-
can be a powerful tool for constructing target-binding MTD variants with equally many varied applications.
+
-
</p> <p>Both the mammalian immune system&#39;s complex defenses and a bacteriophage&#39;s targeting mechanism depend
+
-
upon protein diversification. These models have inspired innovations ranging from targeted drug delivery
+
-
to protein display. Using the major tropism determining (MTD) protein expressed on the Bordatella
+
-
bacteriophage BPP-1, we aim to develop an in vitro system for generating antibody-like proteins that
+
-
bind specified targets. The MTD protein expressed at the phage&#39;s tail fiber is naturally modified at
+
-
its variable region to produce nearly 10<sup>13</sup> possible binding variants while preserving its
+
-
structure. Mutating the MTD&#39;s variable region by PCR can match the massive diversity of MTD in vitro.
+
-
A library of MTD protein-DNA fusions generated by mRNA display can then be screened for binding
+
-
against specified protein targets. This in vitro analog to phage display and immune clonal selection
+
-
can be a powerful tool for constructing target-binding MTD variants with equally many varied applications.
+
-
</p> <p>Both the mammalian immune system&#39;s complex defenses and a bacteriophage&#39;s targeting mechanism depend
+
-
upon protein diversification. These models have inspired innovations ranging from targeted drug delivery
+
-
to protein display. Using the major tropism determining (MTD) protein expressed on the Bordatella
+
-
bacteriophage BPP-1, we aim to develop an in vitro system for generating antibody-like proteins that
+
-
bind specified targets. The MTD protein expressed at the phage&#39;s tail fiber is naturally modified at
+
-
its variable region to produce nearly 10<sup>13</sup> possible binding variants while preserving its
+
-
structure. Mutating the MTD&#39;s variable region by PCR can match the massive diversity of MTD in vitro.
+
-
A library of MTD protein-DNA fusions generated by mRNA display can then be screened for binding
+
-
against specified protein targets. This in vitro analog to phage display and immune clonal selection
+
-
can be a powerful tool for constructing target-binding MTD variants with equally many varied applications.
+
-
</p> <p>Both the mammalian immune system&#39;s complex defenses and a bacteriophage&#39;s targeting mechanism depend
+
-
upon protein diversification. These models have inspired innovations ranging from targeted drug delivery
+
-
to protein display. Using the major tropism determining (MTD) protein expressed on the Bordatella
+
-
bacteriophage BPP-1, we aim to develop an in vitro system for generating antibody-like proteins that
+
-
bind specified targets. The MTD protein expressed at the phage&#39;s tail fiber is naturally modified at
+
-
its variable region to produce nearly 10<sup>13</sup> possible binding variants while preserving its
+
-
structure. Mutating the MTD&#39;s variable region by PCR can match the massive diversity of MTD in vitro.
+
-
A library of MTD protein-DNA fusions generated by mRNA display can then be screened for binding
+
-
against specified protein targets. This in vitro analog to phage display and immune clonal selection
+
-
can be a powerful tool for constructing target-binding MTD variants with equally many varied applications.
+
-
</p> <p>Both the mammalian immune system&#39;s complex defenses and a bacteriophage&#39;s targeting mechanism depend
+
-
upon protein diversification. These models have inspired innovations ranging from targeted drug delivery
+
-
to protein display. Using the major tropism determining (MTD) protein expressed on the Bordatella
+
-
bacteriophage BPP-1, we aim to develop an in vitro system for generating antibody-like proteins that
+
-
bind specified targets. The MTD protein expressed at the phage&#39;s tail fiber is naturally modified at
+
-
its variable region to produce nearly 10<sup>13</sup> possible binding variants while preserving its
+
-
structure. Mutating the MTD&#39;s variable region by PCR can match the massive diversity of MTD in vitro.
+
-
A library of MTD protein-DNA fusions generated by mRNA display can then be screened for binding
+
-
against specified protein targets. This in vitro analog to phage display and immune clonal selection
+
-
can be a powerful tool for constructing target-binding MTD variants with equally many varied applications.
+
-
</p> <p>Both the mammalian immune system&#39;s complex defenses and a bacteriophage&#39;s targeting mechanism depend
+
-
upon protein diversification. These models have inspired innovations ranging from targeted drug delivery
+
-
to protein display. Using the major tropism determining (MTD) protein expressed on the Bordatella
+
-
bacteriophage BPP-1, we aim to develop an in vitro system for generating antibody-like proteins that
+
-
bind specified targets. The MTD protein expressed at the phage&#39;s tail fiber is naturally modified at
+
-
its variable region to produce nearly 10<sup>13</sup> possible binding variants while preserving its
+
-
structure. Mutating the MTD&#39;s variable region by PCR can match the massive diversity of MTD in vitro.
+
-
A library of MTD protein-DNA fusions generated by mRNA display can then be screened for binding
+
-
against specified protein targets. This in vitro analog to phage display and immune clonal selection
+
-
can be a powerful tool for constructing target-binding MTD variants with equally many varied applications.
+
-
</p> </section>
+
-
<ul>
+
-
</html>
+

Revision as of 09:48, 11 September 2013

Retrieved from "http://2013.igem.org/Team:UCLA/HumanPractices"