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Team:UCLA/HumanPractices
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| + | <head><link href='http://fonts.googleapis.com/css?family=Raleway' rel='stylesheet' type='text/css'> | ||
| + | <style type="text/css"> | ||
| + | |||
| + | .bg { | ||
| + | background: url('images/bg_main2.jpg') repeat; | ||
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| + | height: 300%; | ||
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| + | section { | ||
| + | color: black; | ||
| + | font-family: 'Raleway', sans-serif; | ||
| + | width: 750px; | ||
| + | margin: auto; | ||
| + | line-height: 20px; | ||
| + | font-size: 16px; | ||
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| + | <div class="bg"></div> | ||
| + | |||
| + | <section> | ||
| + | <h1>UCLA iGEM</h1> | ||
| + | <p>Both the mammalian immune system's complex defenses and a bacteriophage'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'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'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> | ||
Revision as of 09:41, 11 September 2013
<head><link href='http://fonts.googleapis.com/css?family=Raleway' rel='stylesheet' type='text/css'> <style type="text/css">
.bg {
background: url('images/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>
<section>
UCLA iGEM
Both the mammalian immune system's complex defenses and a bacteriophage'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's tail fiber is naturally modified at its variable region to produce nearly 1013 possible binding variants while preserving its structure. Mutating the MTD'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.
</section>
