Team:Fatih Turkey/Reflectin

From 2011.igem.org

(Difference between revisions)
 
(27 intermediate revisions not shown)
Line 1: Line 1:
<html xmlns="http://www.w3.org/1999/xhtml">
<html xmlns="http://www.w3.org/1999/xhtml">
<head>
<head>
-
<meta http-equiv="Content-Type" content="text/html; charset=utf-8" />
+
<meta http-equiv="Content-Type" content="text/html; charset=UTF-8">
-
<title>Fatih_Turkey</title>
+
<title>deneme baslik</title>
-
<style type="text/css">
+
<style>
-
<!--
+
h1.firstHeading, div#p-logo, div#search-controls, div#contentSub, div#footer-box, div#catlinks{
 +
  display:none;
 +
}
 +
#menubar{
 +
background-color: transparent;
 +
font-size: 85%;
 +
top: 10px;
 +
position: absolute;
 +
margin-top: -12px;
 +
}
 +
 
 +
div#content{
 +
padding: 0 !important;
 +
background: transparent;
 +
border: none !important;
 +
width: auto;
 +
}
 +
 
 +
#menubar li a {
 +
color: #FFFFFF;
 +
background-color: transparent;
 +
}
 +
#globalWrapper{
 +
margin-top:5px;
 +
}
 +
#top-section{
 +
height: 20px !important;
 +
border: none !important;
 +
}
body {
body {
-
background-color: #FFFFFF;
+
font-size: 12px;
 +
font-family: Verdana, Arial, SunSans-Regular, Sans-Serif;
 +
color: #444;
 +
background: #6b6b6b url('https://static.igem.org/mediawiki/igem.org/a/ad/Bg-igem.png');
}
}
-
.style3 {color: #FFFFFF}
+
body,p,pre,div,span{
-
body,td,th {
+
line-height: 160%;
-
font-family: Verdana, Arial, Helvetica, sans-serif;
+
color: #333;
-
color: #FFFFFF;
+
}
}
-
a:link {
+
html, body, div, span, object, iframe, h1, h2, h3, h4, h5, h6, blockquote, pre, a, abbr, acronym, address,
-
text-decoration: none;
+
code, del, dfn, em, img, q, dl, dt, dd, ul, li, fieldset, form, label, legend, table, caption, tbody, tfoot, thead, tr, th, td
 +
{
 +
margin:0;
 +
padding:0;
 +
border:0;
 +
font-weight:inherit;
 +
font-style:inherit;
 +
font-family:inherit;
 +
vertical-align:baseline;
}
}
-
a:visited {
+
 
-
text-decoration: none;
+
em{
 +
font-style:italic;
}
}
-
a:hover {
+
table{
 +
margin-top: 15px;
 +
margin-bottom: 15px;
 +
}
 +
hr{
 +
border: 0;
 +
color: #eee;
 +
background-color: #eee;
 +
height: 1px;
 +
margin-bottom: 20px;
 +
}
 +
img.centered {
 +
display: block;
 +
margin-left: auto;
 +
margin-right: auto;
 +
}
 +
img.alignnone {
 +
margin: 0px 0px 5px 5px;
 +
display: inline;
 +
}
 +
img.alignright {
 +
margin: 0px 0px 5px 10px;
 +
display: inline;
 +
}
 +
 
 +
img.alignleft {
 +
margin: 0px 10px 5px 0px;
 +
display: inline;
 +
}
 +
.alignright {
 +
float: right;
 +
}
 +
 
 +
.alignleft {
 +
float: left;
 +
}
 +
.aligncenter{
 +
margin-left: auto;
 +
margin-right: auto;
 +
}
 +
h1,h2,h3,h4,h5,h6{
 +
  margin-top: 15px;
 +
  margin-bottom: 15px ;
 +
  color: #333;
 +
  line-height: 1.5em;
 +
}
 +
h1 {
 +
font-size: 30px;
 +
}
 +
h2 {
 +
font-size: 25px;
 +
}
 +
h3 {
 +
font-size: 20px;
 +
}
 +
h4 {
 +
font-size: 18px;
 +
}
 +
h5 {
 +
font-size: 16px;
 +
}
 +
 
 +
h6 {
 +
font-size: 15px;
 +
}
 +
a{
text-decoration: none;
text-decoration: none;
}
}
-
a:active {
+
a{
 +
color: #2f86c4;
 +
}
 +
a:hover{
 +
color: #4172ab;
 +
}
 +
#header .logo{
 +
margin-top: 41px;
 +
margin-left: 40px;
 +
}
 +
#footer{
 +
background: #707070;
 +
border-left: 1px #888 solid;
 +
border-right: 1px #888 solid;
 +
width: 988px;
 +
margin: 0px auto 0px;
 +
overflow: hidden;
 +
}
 +
#footer div{
 +
color: #bbb;
 +
}
 +
#footer a{
 +
color: #c4c5cc;
text-decoration: none;
text-decoration: none;
}
}
-
.style6 {color: #000000}
+
#footer a:hover{
-
.style7 {
+
color: #666;
 +
}
 +
 
 +
.footer-sh-wrapper {
 +
    height: 22px;
 +
    margin: auto;
 +
    position: relative;
 +
    width: 990px;
 +
}
 +
.footer-sh-left {
 +
    background: url("https://static.igem.org/mediawiki/2011/b/b7/Footer-sh-left.png") no-repeat scroll 0 0 transparent;
 +
    height: 112px;
 +
    left: 0;
 +
    position: absolute;
 +
    top: -90px;
 +
    width: 10px;
 +
}
 +
.footer-sh {
 +
    background: url("https://static.igem.org/mediawiki/2011/b/bf/Footer-sh.png") repeat-x scroll center bottom #F9F9F9;
 +
    bottom: 0;
 +
    height: 22px;
 +
    left: 10px;
 +
    position: absolute;
 +
    width: 970px;
 +
}
 +
.footer-sh-right {
 +
    background: url("https://static.igem.org/mediawiki/2011/b/b5/Footer-sh-right.png") no-repeat scroll 0 0 transparent;
 +
    height: 112px;
 +
    position: absolute;
 +
    right: 0;
 +
    top: -90px;
 +
    width: 10px;
 +
}
 +
 
 +
.copyright-open{
 +
width: 988px;
 +
height: 0px;
 +
margin:auto;
 +
display: block-inline;
 +
}
 +
h1, h2, h3, h4, h5, h6{
color: #333333;
color: #333333;
 +
}
 +
#header-whole{
 +
 +
position: relative;
 +
z-index: 200;
 +
width: 980px;
 +
margin: 0 auto;
 +
}
 +
#header{
 +
height: 100px;
 +
clear: both;
 +
background: #f9f9f9;
 +
margin: 0 auto;
 +
    width: 970px;
 +
}
 +
#header .logo{
 +
float: left;
 +
margin-top: 15px;
 +
margin-left: 20px;
 +
}
 +
 +
#container{
 +
width: 970px;
 +
margin: 0px auto 0px;
 +
background: none repeat scroll 0 0 #F9F9F9;
 +
}
 +
.copyright-open{
 +
border-top: 1px #a8a8a8 solid;
 +
border-bottom: 1px #888 solid;
 +
border-left: 1px #888 solid;
 +
border-right: 1px #888 solid;
 +
}
 +
.nav-wrapper{
 +
margin: 0px 90px 0px 0px;
 +
float:right;
 +
}
 +
.ddsmoothmenu ul{
 +
padding: 0px;
 +
list-style-type: none;
 +
background: #666666;
 +
}
 +
.ddsmoothmenu ul li{
 +
position: relative;
 +
display: block;
 +
float: left;
 +
}
 +
.ddsmoothmenu ul li a{
 +
line-height: 140%;
 +
overflow: hidden;
 +
text-align: left;
 +
font-family: 'Lucida Grande', Arial, Verdana, sans-serif;
 +
word-spacing: 1px;
font-size: 14px;
font-size: 14px;
 +
font-weight: normal;
 +
display: block; /*background of menu items (default state)*/
 +
padding: 34px 20px 10px 17px;
 +
text-decoration: none;
}
}
-
.style8 {color: #000000; font-size: 12px; }
+
.ddsmoothmenu ul li a span {
-
.style10 {
+
font-weight: normal;
-
color: #000000;
+
color: #888;
-
font-size: 24px;
+
font-size: 10px;
-
font-weight: bold;
+
clear: both;
 +
display:block;
 +
width: 60px;
 +
}
 +
* html .ddsmoothmenu ul li a{ /*IE6 hack to get sub menu links to behave correctly*/
 +
display: inline-block;
}
}
-
-->
 
-
</style></head>
 
 +
.ddsmoothmenu ul li a:link, .ddsmoothmenu ul li a:visited{
 +
color: #333;
 +
}
 +
 +
.ddsmoothmenu ul li a.selected{ /*CSS class that's dynamically added to the currently active menu items' LI A element*/
 +
color: #888;
 +
}
 +
 +
.ddsmoothmenu ul li a:hover{
 +
color: #888;
 +
}
 +
 +
/*1st sub level menu*/
 +
.ddsmoothmenu ul li ul{
 +
position: absolute;
 +
left: 0;
 +
visibility: hidden;
 +
display: none; /*collapse all sub menus to begin with*/
 +
border: 1px #222 solid;
 +
-webkit-box-shadow: rgba(0, 0, 0, 0.2) 0px 0px 2px 1px;
 +
-moz-box-shadow: rgba(0, 0, 0, 0.2) 0px 0px 2px 1px;
 +
box-shadow: rgba(0, 0, 0, 0.2) 0px 0px 2px 1px;
 +
}
 +
 +
/*Sub level menu list items (undo style from Top level List Items)*/
 +
.ddsmoothmenu ul li ul li{
 +
text-align:left;
 +
float: none;
 +
background: url('img/bg-menu2.png');
 +
}
 +
 +
.ddsmoothmenu ul li ul li a{
 +
color: #fff;
 +
font-size: 12px;
 +
}
 +
.ddsmoothmenu ul li ul li  a.selected{ /*CSS class that's dynamically added to the currently active menu items' LI A element*/
 +
color: #fff;
 +
}
 +
.ddsmoothmenu ul li ul li a:link, .ddsmoothmenu ul li ul li a:visited{
 +
color: #fff;
 +
}
 +
.ddsmoothmenu ul li ul li a:hover{
 +
color: #ffc;
 +
}
 +
.ddsmoothmenu ul li ul li ul{
 +
top: 0;
 +
}
 +
 +
/* Sub level menu links style */
 +
.ddsmoothmenu ul li ul li a{
 +
width: 160px; /*width of sub menus*/
 +
padding: 0px 0px 0px 10px;
 +
height: 38px;
 +
line-height: 320%;
 +
border-left: 1px #555 solid;
 +
overflow: hidden;
 +
}
 +
 +
/* Holly Hack for IE \*/
 +
* html .ddsmoothmenu{height: 1%;} /*Holly Hack for IE7 and below*/
 +
 +
.copyright{
 +
width: 930px;
 +
color: #959595;
 +
background: #eee;
 +
clear: both;
 +
line-height: 190%;
 +
text-align: right;
 +
padding: 10px 20px 10px;
 +
margin: 0px auto 0px;
 +
}
 +
.copyright a{
 +
color: #bbb;
 +
text-decoration: none;
 +
}
 +
.copyright a:hover{
 +
color: #ccc;
 +
}
 +
.bar-title-whole{
 +
overflow: visible;
 +
position: relative;
 +
width: 990px;
 +
margin: auto;
 +
z-index: 10;
 +
}
 +
.bar-title{
 +
background: #999 url('https://static.igem.org/mediawiki/2011/e/e9/Bar-title-bg.jpg') top;
 +
border-left: 1px #8a8a8a solid;
 +
border-right: 1px #8a8a8a solid;
 +
 +
width: 918px;
 +
height: 122px;
 +
margin: auto;
 +
overflow: hidden;
 +
padding-left: 35px;
 +
padding-right: 35px;
 +
color: #ddd;
 +
line-height: 150%;
 +
font-size: 12px;
 +
 +
position: relative;
 +
z-index: 10;
 +
}
 +
 +
.bar-title h2{
 +
color: #fff;
 +
margin-top: 15px;
 +
margin-bottom: 30px !important;
 +
}
 +
.bar-title h5{
 +
color: #eee;
 +
}
 +
.bar-title-sh-left{
 +
width: 10px;
 +
height: 112px;
 +
background: url('https://static.igem.org/mediawiki/2011/6/69/Bar-title-sh-left.png') no-repeat;
 +
display: block-inline;
 +
position: absolute;
 +
top: 122px;
 +
left: 0px;
 +
}
 +
.bar-title-sh{
 +
width: 970px;
 +
height: 8px;
 +
background: url('https://static.igem.org/mediawiki/2011/3/37/Bar-title-sh.png') repeat-x;
 +
display: block-inline;
 +
position: absolute;
 +
top: 122px;
 +
left: 10px;
 +
}
 +
.bar-title-sh-right{
 +
width: 10px;
 +
height: 112px;
 +
background: url('https://static.igem.org/mediawiki/2011/c/c6/Bar-title-sh-right.png') no-repeat;
 +
display: block-inline;
 +
position: absolute;
 +
top: 122px;
 +
right: 0px;
 +
}
 +
#page{
 +
    width: 970px;
 +
    margin: 0px auto 0px;
 +
    overflow: hidden;
 +
    background: #f9f9f9;
 +
   
 +
}
 +
 +
#page .page-wrapper{
 +
margin: 15px 30px 0px 30px;
 +
width: 910px;
 +
overflow: hidden;
 +
float: left;
 +
}
 +
#page .page-wrapper-right{
 +
margin: 30px 40px 0px 25px;
 +
width: 935px;
 +
overflow: hidden;
 +
float: right;
 +
}
 +
#page .title-wrapper h1{
 +
margin-top: 0.5em;
 +
margin-bottom: 0.3em;
 +
}
 +
#page .meta-left-full{
 +
margin: 15px 0px 5px 0px;
 +
overflow: hidden;
 +
}
 +
#page .meta-left-button{
 +
margin: 5px 0px 60px 0px;
 +
overflow: hidden;
 +
}
 +
#page .w600{
 +
width: 600px;
 +
}
 +
 +
</style>
 +
 +
 +
</head>
<body>
<body>
-
<table width="969" border="0" align="center">
+
<script type="text/javascript" src="http://simsekburak.com/fatihigem/ddsmoothmenu.js"></script>
-
  <tr>
+
 
-
    <td width="963" height="216" align="center" valign="middle" background="https://static.igem.org/mediawiki/2011/0/02/Renkli.jpg">&nbsp;</td>
+
<script>
-
  </tr>
+
$(document).ready(
-
  <tr>
+
ddsmoothmenu.init({
-
    <td height="53" bgcolor="#FFFFFF"><table width="961" border="0" cellspacing="10" bgcolor="#FFFFFF">
+
mainmenuid: "topmenu",
-
        <tr>
+
orientation: 'h',
-
          <td width="200" align="center" valign="middle" bgcolor="#990000"><a href="index.html"><span class="style3">HOME</span></a></td>
+
classname: 'ddsmoothmenu',
-
          <td width="205" align="center" valign="middle" bgcolor="#695E0E"><a href="canvastown.html"><span class="style3">CANVAS&nbsp; TOWN</span></a></td>
+
contentsource: "markup"
-
          <td width="257" align="center" valign="middle" bgcolor="#1D3551"><a href="therainbowgraveyard.html"><span class="style3">THE RAINBOW GRAVEYARD</span></a></td>
+
}));
-
          <td width="309" align="center" valign="middle" bgcolor="#960C47"><a href="notebook.html"><span class="style3">&nbsp;NOTEBOOK</span></a></td>
+
 
-
        </tr>
+
jQuery(window).load(function() {
-
        <tr>
+
setTimeout(function(){
-
          <td height="20" colspan="4" align="center" valign="middle" bgcolor="#1D3551">REFLECTIN</td>
+
jQuery('#slider').nivoSlider({
-
        </tr>
+
pauseTime:4000,
-
    </table></td>
+
animSpeed:600,
-
  </tr>
+
captionOpacity: 0.8,
-
  <tr>
+
pauseOnHover:true,
-
    <td height="778" align="center" valign="top" bgcolor="#FFFFFF"><table width="832" border="0">
+
directionNav:true,
-
      <tr>
+
directionNavHide:true,
-
        <td height="47" align="center" valign="middle"><span class="style10">REFLECTIN</span></td>
+
controlNavThumbs:true,
-
      </tr>
+
controlNavThumbsFromRel:true,
-
      <tr>
+
});
-
        <td width="826" height="61" align="center" valign="top"><p align="justify" class="style6">&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp; Many cephalopods(squid, cuttlefish, octopus)  exhibit remarkable dermal  iridescence (more than meets the eye), a component of their complex,dynamic camouflage and communication. In the species Euprymna scolopes, the light organ iridescence is static and is due to reflectin protein-based platelets assembled into lamellar thin-film reflectors called iridosomes, contained within iridescent cells called iridocytes.<br />
+
}, 1000),
-
          Reflectin hierarchical protein assembly is necessity for the responsive, tunable optical function of iridosome cells. This protein assembly can be triggered by chemical stimulation and that assembly can be reversible and fine-tuned.<br />
+
setTimeout(function(){
-
        &nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp; Namely reflectin proteins were identified as the major biomaterial component of iridosomes. The RA1 gene in The Rainbow Graveyard Project was artificially synthesized into pBluescript to transform into E. coli. In addition, Kramer et al. (2007) isolated <span class="style6">reflectin proteins exhibit unusual solubility and selfassociation properties.<br />
+
/* For slider shortcode */
-
 &nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp; Self-association of RA1 is likely to stem from a combination of   electrostatic and weak aromatic interactions. Reflectins are, indeed, characterized by their high content of polar aromatic residues and arginines, and several lines of evidence suggest that they are intrinsically unstructured, with no likely transmembrane, alphahelix or beta-sheet regions. E. scolopes reflectins also have high arginine, hydrophobic aromatic content and ‘methionine-rich membrane-associated proteins’. It’s demonstrated that they have a high affinity for assembly with microsomal membranes.<br />
+
jQuery('#slider2').nivoSlider({
-
&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;
+
pauseTime:4000,
-
The mechanism of reflectance is the same as that of coloured soap bubbles. If the soap film (or  multilayer plate) is very thin, shorter wavelengths are reflected, e.g. blue light; if it is thicker, longer wavelengths, such as yellow and red, are reflected. <br />
+
animSpeed:600,
-
The reflectin proteins that apparently change their conformation or assembly to reversibly create the photonic structure.<br />
+
captionOpacity: 0.8,
-
          </span></p>         </td>
+
pauseOnHover:true,
-
      </tr>
+
directionNavHide:true });
-
    </table>     
+
}, 1000);
-
      <table width="489" height="161" border="0">
+
-
        <tr>
+
});
-
          <td width="297"><img src="reflektin1.png" width="297" height="221" /></td>
+
</script>
-
          <td width="198"><p align="center" class="style7">Reflector, formed of a highly  organized  multilayer of collagen rods that reflect  specific wavelengths </p></td>
+
 
-
        </tr>
+
<div class="body-2">
-
      </table>     
+
<!-- Header -->
-
      <table width="381" height="91" border="0">
+
<div id="header-whole">
-
        <tr>
+
<div id="header">
-
          <td width="375"><img src="reflektin2.png" width="367" height="168" /></td>
+
<a href="https://2011.igem.org/" style="position:absolute; right:10px; top:5px;"><img src="https://static.igem.org/mediawiki/2011/9/9c/Igem_basic_logo.png"/></a>
-
        </tr>
+
<!-- Logo -->
-
      </table>
+
<div>
-
      <table width="830" border="0">
+
<div class="logo">
-
        <tr>
+
<a href="https://2011.igem.org/Team:Fatih_Turkey">
-
          <td width="824"><p align="justify" class="style6">&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp; Multilayer reflector that appears red at near-normal viewing angles will appear first yellow, then green and blue at increasingly oblique angles.  
+
<img width="258" src="https://static.igem.org/mediawiki/2011/b/b6/Fatih_turkey_logo.png">
-
            This dynamic reflection occur by altering platelet and  
+
</a>
-
            inter-platelet thicknesses in the multilayer reflector and/or altering  
+
</div>
-
            the overall effective refractive index of the intra-platelet material. This allows the entire visible spectrum to be reflected from a single  
+
</div>
-
            platelet stack.  
+
<!-- Menu -->
-
            The increase in film thickness resulted in detectable redshift  
+
<div class="nav-wrapper">
-
            of the visible spectra and dominated any effect of decreasing  
+
<div class="nav-main">
-
            refractive index owing to water sorption, which would have caused  
+
<div id="topmenu" class="ddsmoothmenu">
-
            a blue-shift in the spectrum  
+
<ul id="menu-main" class="menu">
-
            Kramer et al. (2007) have performed Micro-dialysis of reflectin 1a into various buffers, which resulted  
+
<li>
-
            in two general types of aggregative structures. Optically clear  
+
<a href="https://2011.igem.org/Team:Fatih_Turkey">Home</a>
-
            bulk precipitation was seen in non-reducing conditions  
+
</li>
-
            and filamentous protein structures were observed in reducing  
+
<li>
-
            conditions controlled through the addition of a 10:1  
+
<a href="https://2011.igem.org/Team:Fatih_Turkey/Project">Project</a>
-
            ratio of reduced to oxidized glutathione  
+
<ul>
-
            After several weeks at  
+
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Project">Overall Project</a></li>
-
            4 ◦C, the filamentous structures formed a webbed structure that  
+
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/LALF">LALF</a></li>
-
            resulted in the supramolecular assembly of thin ribbons  
+
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Reflectin">Reflectin</a></li>
-
            </p>
+
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Biofilm">Biofilm</a></li>
-
            <p class="style6">&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp; In our project, we use reflectin 1a for detecting survival   of E.coli. Both of our bacteria (E.coli and B.subtilis) are expected to synthesize reflectin. When the biofilm containing anti-LPS factor (LALF) from  B.subtilis, it will bind to LPS on Gram (-) bacteria’s cell wall (E.coli in our project) and so Gram (-) bacteria will not grow and survive in our biofilm surface. Around the binding, reflectin thickness is going to decrease and  change the surface colours because of E.coli’s death. So if the colour changes from red to blue, we can say there was a contact between E.coli and B.subtilis via anti-LPS factor.<br />
+
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Experiments">Experiments</a></li>
-
            You can see <a href="https://2011.igem.org/Team:Fatih_Turkey/Anti_LPS">https://2011.igem.org/Team:Fatih_Turkey/Anti_LPS</a>&nbsp; for more information about LALF.</p>
+
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Parts">Parts</a></li>
-
          </td>
+
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Future_Plan">Future Plan</a></li>
-
        </tr>
+
</ul>
-
      </table>
+
</li>
-
      <p>&nbsp;</p>
+
<li>
-
      <table width="501" border="0">
+
<a href="https://2011.igem.org/Team:Fatih_Turkey/Data_Page">Data Page</a>
-
        <tr>
+
</li>
-
          <td width="521"><p align="justify" class="style8">REFENCES</p>
+
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Team">Team</a>
-
            <p align="justify" class="style8">1)nature materials VOL 6 JULY 2007<br />
+
<ul>
-
              (Review.The self-organizing properties of squid reflectin protein, Ryan M. Kramer et al.) <br />
+
                                                                                <li><a
-
              Published online: 3 June 2007; doi:10.1038/nmat1930</p>
+
href="https://2011.igem.org/Team:Fatih_Turkey/Members">Members</a></li>
-
            <p align="justify" class="style8">2)J. R. Soc. Interface (2009) 6, S149–S163<br />
+
                                                                                  <li><a
-
              doi:10.1098/rsif.2008.0366.focus<br />
+
href="https://2011.igem.org/Team:Fatih_Turkey/Gallery">Gallery</a></li>
-
              Published online 15 December 2008<br />
+
                                                                                  <li><a
-
              (Review. Structural coloration in cephalopods L. M. Ma¨thger et al. S155)</p>
+
href="https://2011.igem.org/Team:Fatih_Turkey/Europe_Jamboree">Europe Jamboree</a></li>
-
            <p align="justify" class="style8">3)Review. Structural coloration in cephalopods L. M. Ma¨thger et al. S161<br />
+
</ul>
-
            </p>
+
</li>
-
            <p align="justify" class="style8">4)DOI: 10.1126/science.1091288<br />
+
<li>
-
              <em>Science </em>303, 235 (2004);<br />
+
<a href="https://2011.igem.org/Team:Fatih_Turkey/Human_Practice">Human Practice</a>
-
              Wendy J. Crookes<em>, et al.(</em>www.sciencemag.org SCIENCE VOL303 9 JANUARY 2004)<br />
+
<ul>
-
            </p>
+
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Sporocide">Sporicide</a></li>
-
            <p align="justify" class="style8">5)A.R. Tao et al. / Biomaterials 31 (2010) 793–801<br />
+
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/iGEM_for_7_to_77">iGEM for 7 to 77</a></li>
-
            </p>
+
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/game">Game</a></li>
-
            <p align="justify" class="style8">6)J. R. Soc. Interface (2010) 7, 549–560 <br />
+
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/canvas_times">Canvas Times</a></li>
-
              doi:10.1098/rsif.2009.0299<br />
+
                                                                                <li><a
-
          Published online 23 September 2009(Reflectin phosphorylation M. Izumi et al.)</p>
+
href="https://2011.igem.org/Team:Fatih_Turkey/Safety">Safety</a></li>
-
          <p class="style8">&nbsp;</p></td>
+
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/collaboration">Collaboration</a></li>
-
        </tr>
+
</ul>
-
      </table>    
+
</li>
-
      <p>&nbsp;</p>
+
<li>
-
    </td>
+
<a href="https://2011.igem.org/Team:Fatih_Turkey/Lab_Garage">Lab Garage</a>
-
  </tr>
+
<ul>
-
</table>
+
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Notebook">Notebook</a></li>
 +
<li><a href="https://2011.igem.org/Team:Fatih_Turkey/Procedures">Procedures</a></li>
 +
</ul>
 +
</li>
 +
                                                            </ul>
 +
</div>
 +
</div>
 +
</div>
 +
</div>
 +
</div>
 +
<!-- End Header -->
 +
<div class="bar-title-whole">
 +
  <div class="bar-title">
 +
      <h2 style="font-family: Verdana, Arial, SunSans-Regular, sans-serif;">Project</h2>
 +
      <h5 style="font-family: Verdana, Arial, SunSans-Regular, sans-serif;">Reflectin</h5>
 +
    </div>
 +
  <div class="bar-title-sh-left"></div>
 +
  <div class="bar-title-sh"></div>
 +
  <div class="bar-title-sh-right"></div>
 +
        </div>
 +
</div>
 +
<div id="container">
 +
<div id="page">
 +
<div class="page-wrapper">
 +
<!-- post container -->
 +
<div>
 +
<div class="meta-left-full">
 +
 
 +
 
 +
 
 +
 
 +
<p><strong>Reflectin</strong><br />
 +
  Many cephalopods (squid, cuttlefish, octopus etc.) exhibit remarkable dermal iridescence (more than meets the eye), a component of their complex, dynamic camouflage and communication. In the species Euprymna scolopes, the light organ iridescence is static and is due to reflectin protein-based platelets assembled into lamellar thin-film reflectors called iridosomes, contained within iridescent cells called iridocytes.<br />
 +
  Reflectin hierarchical protein assembly is necessity for the responsive, tunable optical function of iridosome cells. This protein assembly can be triggered by chemical stimulation and that assembly can be reversible and fine-tuned.<br />
 +
  Namely reflectin proteins were identified as the major biomaterial component of iridosomes. The RA1 gene in The Rainbow Graveyard Project was artificially synthesized into pBluescript to transform into E. coli. In addition, Kramer et al. (2007) isolated reflectin proteins exhibit unusual solubility and self-association properties.</p>
 +
<p>                                                                   <img src="https://static.igem.org/mediawiki/2011/2/20/Reflectinhkjljk..png" alt="Reflectinhkjljk..png (458×274)" /> <br />
 +
  Self-association of RA1 is likely to stem from a combination of electrostatic and weak aromatic interactions. Reflectins are, indeed, characterized by their high content of polar aromatic residues and arginines, and several lines of evidence suggest that they are intrinsically unstructured, with no likely transmembrane, alphahelix or beta-sheet regions. E. scolopes reflectins also have high arginine, hydrophobic aromatic content and “methionine-rich membrane-associated proteins”. It is demonstrated that they have a high affinity for assembly with microsomal membranes.<br />
 +
  The mechanism of reflectance is the same as that of colored soap bubbles. If the soap film (or multilayer plate) is very thin, shorter wavelengths are reflected, e.g. blue light; if it is thicker, longer wavelengths, such as yellow and red, are reflected. The reflectin proteins that apparently change their conformation or assembly to reversibly create the photonic structure.</p>
 +
<p>                                                                     <img src="https://static.igem.org/mediawiki/2011/1/19/Reflectn1ujh%C4%B1s.png" alt="Reflectn1ujhıs.png (451×222)" /></p>
 +
<p>Multilayer reflector that appears red at near-normal viewing angles will appear first yellow, then green and blue at increasingly oblique angles. This dynamic reflection occurs by altering platelet and inter-platelet thicknesses in the multilayer reflector and/or altering the overall effective refractive index of the intra-platelet material. This allows the entire visible spectrum to be reflected from a single platelet stack. The increase in film thickness resulted in detectable redshift of the visible spectra and dominated any effect of decreasing refractive index owing to water sorption, which would have caused a blue-shift in the spectrum Kramer et al. (2007) have performed Micro-dialysis of reflectin 1a into various buffers, which resulted in two general types of aggregative structures. Optically clear bulk precipitation was seen in non-reducing conditions and filamentous protein structures were observed in reducing conditions controlled through the addition of a 10:1 ratio of reduced to oxidized glutathione .After several weeks at 4 ◦C, the filamentous structures formed a webbed structure that resulted in the supramolecular assembly of thin ribbons.</p>
 +
<p><img src="https://static.igem.org/mediawiki/2011/5/50/Reflectnkjmld%C5%9Fkas.png" alt="Reflectnkjmldşkas.png (405×445)" width="353" height="384" align="middle" /><img src="https://static.igem.org/mediawiki/2011/2/27/Squid_021005_42.png" alt="Squid_021005_42.jpg (500×386)" width="502" height="386" align="top" /><br />
 +
 
 +
</p>
 +
<p>In our project, we use reflectin 1A for detecting the survival of E.coli. Both of our bacteria (E.coli and B.subtilis) are expected to synthesize reflectin. As LALF is being produced by B.subtilis, both bacteria will synthesize reflectin. Meanwhile, LALF will bind to cell wall of gram negative bacterium (E.coli in our project). Therefore, gram (-) bacteria will not grow and survive in our biofilm surface. During the binding process, production of reflectin layer is going to decrease. Because of this, color of the surface will change due to the light reflecting ability of reflectin depending on the thickness of its layer. So, if the colour changes from red to blue, we can say there was a contact between E.coli and B.subtilis via anti-LPS factor.</p>
 +
 
 +
 
 +
 
 +
<h3>REFERENCES</h3>
 +
<ol>
 +
<li>nature materials VOL 6 JULY 2007
 +
(Review.The self-organizing properties of squid reflectin protein, Ryan M. Kramer et al.)  
 +
Published online: 3 June 2007; doi:10.1038/nmat1930</li>
 +
<li>J. R. Soc. Interface (2009) 6, S149–S163
 +
doi:10.1098/rsif.2008.0366.focus
 +
Published online 15 December 2008
 +
(Review. Structural coloration in cephalopods L. M. Ma¨thger et al. S155)</li>
 +
<li>Review. Structural coloration in cephalopods L. M. Ma¨thger et al. S161</li>
 +
<li>DOI: 10.1126/science.1091288
 +
Science 303, 235 (2004);
 +
Wendy J. Crookes, et al.(www.sciencemag.org SCIENCE VOL303 9 JANUARY 2004)</li>
 +
<li>A.R. Tao et al. / Biomaterials 31 (2010) 793–801</li>
 +
<li>J. R. Soc. Interface (2010) 7, 549–560  
 +
doi:10.1098/rsif.2009.0299
 +
Published online 23 September 2009(Reflectin phosphorylation M. Izumi et al.)</li>
 +
</ol>
 +
</div>
 +
    </div>
 +
      </div>
 +
</div>
 +
</div>
 +
 
 +
<div class="footer-sh-wrapper">
 +
<div class="footer-sh-left"></div>
 +
<div class="footer-sh"></div>
 +
<div class="footer-sh-right"></div>
 +
</div>
 +
<div id="footer">
 +
<style>
 +
#footer img:hover{
 +
opacity:0.6;
 +
}
 +
</style>
 +
<div>
 +
<h3 style="color:#BBB;">Sponsors</h3>
 +
<img height="100" src="https://static.igem.org/mediawiki/2011/7/72/Tubitak_-_Kopya.png"/>
 +
<a href="http://www.sentegen.com">
 +
<img height="100" src="https://static.igem.org/mediawiki/2011/2/2d/Sentegennnn.png"/></a>
 +
</div>
 +
</div>
 +
<div class="copyright-open">
 +
</div>
 +
<div class="copyright">
 +
2011 © Fatih Medical School
 +
</div>
 +
</div>
 +
 
 +
 
</body>
</body>
</html>
</html>

Latest revision as of 01:13, 29 October 2011

deneme baslik

Project

Reflectin

Reflectin
Many cephalopods (squid, cuttlefish, octopus etc.) exhibit remarkable dermal iridescence (more than meets the eye), a component of their complex, dynamic camouflage and communication. In the species Euprymna scolopes, the light organ iridescence is static and is due to reflectin protein-based platelets assembled into lamellar thin-film reflectors called iridosomes, contained within iridescent cells called iridocytes.
Reflectin hierarchical protein assembly is necessity for the responsive, tunable optical function of iridosome cells. This protein assembly can be triggered by chemical stimulation and that assembly can be reversible and fine-tuned.
Namely reflectin proteins were identified as the major biomaterial component of iridosomes. The RA1 gene in The Rainbow Graveyard Project was artificially synthesized into pBluescript to transform into E. coli. In addition, Kramer et al. (2007) isolated reflectin proteins exhibit unusual solubility and self-association properties.

                                                                   Reflectinhkjljk..png (458×274) 
Self-association of RA1 is likely to stem from a combination of electrostatic and weak aromatic interactions. Reflectins are, indeed, characterized by their high content of polar aromatic residues and arginines, and several lines of evidence suggest that they are intrinsically unstructured, with no likely transmembrane, alphahelix or beta-sheet regions. E. scolopes reflectins also have high arginine, hydrophobic aromatic content and “methionine-rich membrane-associated proteins”. It is demonstrated that they have a high affinity for assembly with microsomal membranes.
The mechanism of reflectance is the same as that of colored soap bubbles. If the soap film (or multilayer plate) is very thin, shorter wavelengths are reflected, e.g. blue light; if it is thicker, longer wavelengths, such as yellow and red, are reflected. The reflectin proteins that apparently change their conformation or assembly to reversibly create the photonic structure.

                                                                     Reflectn1ujhıs.png (451×222)

Multilayer reflector that appears red at near-normal viewing angles will appear first yellow, then green and blue at increasingly oblique angles. This dynamic reflection occurs by altering platelet and inter-platelet thicknesses in the multilayer reflector and/or altering the overall effective refractive index of the intra-platelet material. This allows the entire visible spectrum to be reflected from a single platelet stack. The increase in film thickness resulted in detectable redshift of the visible spectra and dominated any effect of decreasing refractive index owing to water sorption, which would have caused a blue-shift in the spectrum Kramer et al. (2007) have performed Micro-dialysis of reflectin 1a into various buffers, which resulted in two general types of aggregative structures. Optically clear bulk precipitation was seen in non-reducing conditions and filamentous protein structures were observed in reducing conditions controlled through the addition of a 10:1 ratio of reduced to oxidized glutathione .After several weeks at 4 ◦C, the filamentous structures formed a webbed structure that resulted in the supramolecular assembly of thin ribbons.

Reflectnkjmldşkas.png (405×445)Squid_021005_42.jpg (500×386)

In our project, we use reflectin 1A for detecting the survival of E.coli. Both of our bacteria (E.coli and B.subtilis) are expected to synthesize reflectin. As LALF is being produced by B.subtilis, both bacteria will synthesize reflectin. Meanwhile, LALF will bind to cell wall of gram negative bacterium (E.coli in our project). Therefore, gram (-) bacteria will not grow and survive in our biofilm surface. During the binding process, production of reflectin layer is going to decrease. Because of this, color of the surface will change due to the light reflecting ability of reflectin depending on the thickness of its layer. So, if the colour changes from red to blue, we can say there was a contact between E.coli and B.subtilis via anti-LPS factor.

REFERENCES

  1. nature materials VOL 6 JULY 2007 (Review.The self-organizing properties of squid reflectin protein, Ryan M. Kramer et al.) Published online: 3 June 2007; doi:10.1038/nmat1930
  2. J. R. Soc. Interface (2009) 6, S149–S163 doi:10.1098/rsif.2008.0366.focus Published online 15 December 2008 (Review. Structural coloration in cephalopods L. M. Ma¨thger et al. S155)
  3. Review. Structural coloration in cephalopods L. M. Ma¨thger et al. S161
  4. DOI: 10.1126/science.1091288 Science 303, 235 (2004); Wendy J. Crookes, et al.(www.sciencemag.org SCIENCE VOL303 9 JANUARY 2004)
  5. A.R. Tao et al. / Biomaterials 31 (2010) 793–801
  6. J. R. Soc. Interface (2010) 7, 549–560 doi:10.1098/rsif.2009.0299 Published online 23 September 2009(Reflectin phosphorylation M. Izumi et al.)
2011 © Fatih Medical School

Retrieved from "http://2011.igem.org/Team:Fatih_Turkey/Reflectin"