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quantificacao.html
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<!DOCTYPE html>
<html lang="prt-br"> <!-- português -->
<head>
<meta charset="utf-8"> <!-- caracteres especiais -->
<meta http-equiv="X-UA-Compatible" content="IE=edge,chrome=1"> <!-- Permite usar o plug-in do Google Chrome que tem um mecanismo rápido de JavaScript ao abrir páginas no navegador -->
<title>FluxPRT</title> <!-- nome do Guia Interativo FluxPRT -->
<meta name="description" content="">
<meta name="viewport" content="width=device-width, initial-scale=1.0"> <!-- permite controlar a janela de visualização, reduzindo a página web inteira para caber na tela de celulares e ipads-->
<link rel="apple-touch-icon" href="apple-touch-icon.png"> <!-- Adapta os icones para vários dispositivos da apple-->
<!-- arquivos CSS -->
<link rel="stylesheet" href="css/bootstrap.min.css">
<link rel="stylesheet" href="css/bootstrap-theme.min.css">
<link rel="stylesheet" href="css/fontAwesome.css">
<link rel="stylesheet" href="css/light-box.css">
<link rel="stylesheet" href="css/owl-carousel.css">
<link rel="stylesheet" href="css/templatemo-style.css">
<link href="https://fonts.googleapis.com/css?family=Open+Sans:300,400,600,700,800" rel="stylesheet"> <!-- chamar a familia da fonte OpenSans -->
<script src="js/vendor/modernizr-2.8.3-respond-1.4.2.min.js"></script> <!-- biblioteca de js que detecta os recursos disponíveis no navegador e informa quando o navegador não é compatível -->
</head>
<body>
<header class="nav-down responsive-nav hidden-lg hidden-md">
<button type="button" id="nav-toggle" class="navbar-toggle" data-toggle="collapse" data-target="#main-nav">
<span class="sr-only">Toggle navigation</span> <!-- têcnica usada para acessibilidade-->
<span class="icon-bar"></span>
<span class="icon-bar"></span>
<span class="icon-bar"></span>
</button>
<!-- cabecalho da barra de navegação /navbar-header/ -->
<div id="main-nav" class="collapse navbar-collapse"><nav><ul class="nav navbar-nav">
<li><a href="#top">Cadastro do Experimento</a></li>
<li><a href="#video">Fluxo de trabalho</a></li>
<li><a href="#blog">Objetivo do Experimento</a></li>
<li><a href="#contact">e-book</a></li>
</ul></nav>
</div>
</header>
<div class="sidebar-navigation hidde-sm hidden-xs">
<div class="logo">
<a href="index.html"><em>Flux</em>PRT</a>
</div>
<nav>
<ul>
<li>
<a href="#video">
<em>Cadastro do Experimento</em>
</a>
</li>
<li>
<a href="#video">
<span class="rect"></span>
<span class="circle"></span>
Fluxo de trabalho
</a>
</li>
</li>
<li>
<a href="#blog">
<span class="rect"></span>
<span class="circle"></span>
Objetivo do Experimento
</a>
</li>
<li>
<a href="#contact">
<span class="rect"></span>
<span class="circle"></span>
e-book
</a>
</li>
</ul>
</nav>
<ul class="social-icons">
<!-- página inicial da página web -->
<li><a href="index.html"><i class="fa fa-home"></i></a></li>
<!-- github do guia FluxPRT -->
<li><a href="http://cabernet.luar.dcc.ufmg.br:7070/groups/luar" target="_blank"><i class="fa fa-github"></i></a></li>
<!-- webpage do LUAR -->
<li><a href="http://luar.dcc.ufmg.br/" target="_blank"><i class="fa fa-share-alt"></i></a></li>
<!-- email da desenvolvedora -->
<li><a href="mailto:elizabeth.espinoza@ufv.br" target="_blank"><i class="fa fa-envelope"></i></a></li>
</ul>
</div>
<div class="page-content">
<section id="video" class="content-section">
<div class="row"><div class="col-md-12"><div class="section-heading">
<h1>Você está na atividade <em>Cadastro do Experimento</em> do FluxPRT</h1>
<p>O Guia Interativo do FluxPRT segue o Fluxo de Trabalho em Proteômica.</p>
</div>
<div class="text-content">
<p>O Guia Interativo do FluxPRT segue o Fluxo de Trabalho em Proteômica apresentado a seguir, clique nas atividades enumeradas mais detalhes e dicas. Aproveite instruções e dicas para tornar sua experiência com o FluxPRT ainda mais produtiva, nesta seção sao apresentadas informacões a respeito do Cadastro do Experimento.<br><br></p>
</div>
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</section>
<section id="blog" class="content-section">
<div class="section-heading">
<h1><em>Objetivo</em><br>do Experimento</h1><p>Sua pergunta biológica e objetivo precisam ser claramente definidos.<br>Fatores a considerar.</p>
</div>
<div class="section-content"><div class="tabs-content"><div class="wrapper">
<ul class="tabs clearfix" data-tabgroup="first-tab-group">
<li><a href="#tab1" class="active">Quantidade</a></li>
<li><a href="#tab2">Atividade</a></li>
<li><a href="#tab3">Pureza</a></li>
<li><a href="#tab4">Fonte</a></li>
<li><a href="#tab5">Literatura</a></li>
</ul>
<section id="first-tab-group" class="tabgroup">
<!-- quantidade -->
<div id="tab1"><ul><li><div class="item">
<div class="text-content">
<h4>Qual quantidade preciso de proteína?</h4>
<span>Fatores a considerar</span>
<p>Para alcançar o objetivo do seu experimento poderá ser necessário diferentes quantidades de proteína, veja aqui alguns exemplos:<br><ol>
<li><em>Análise Físico-Química Completa:</em> centenas de proteínas purificadas (Wingfield, 2015).</li>
<li><em>Análise cinética da catálise enzimática:</em> poucos miligramas.</li>
<li><em>Anticorpos policlonais:</em> menos de 1 miligrama (Liu, Ma, Winter, and Bayer, 2010).</li>
<li><em>Obter informação do extremo N-terminal da sequência de proteína:</em> poucas microgramas.</li>
</ol></p>
<p>Uma estratégia interessante é optar nas primeiras etapas pelas técnicas de alta capacidade mas debaixo poder de resolução, e após ter o volume e quantidade de proteína necessários, usar técnicas de alta resolução. No entanto, se precisar de pouca quantidade de proteínas pode se optar pelas técnicas de alta resolução (BioProcess-Media, 2003).</p>
</div></div></li></ul></div>
<!-- //quantidade -->
<!-- atividade -->
<div id="tab2"><ul><li><div class="item">
<div class="text-content">
<h4>Preciso conservar a atividade biológica da proteína?</h4>
<span>Conheça o seu experimento</span>
<p>Se sua resposta é sim, precisa fazer o menor número de passos possível com uma mínima troca de solução tampão e fique atento nas modificações químicas que podem acontecer na etapa de clivagem proteolítica, que pode afetar a atividade da proteína (Labrou, 2020). Se sua resposta é negativa, não vai precisar de muita restrição dos métodos de purificação.</p>
</div></div></li></ul></div>
<!-- //atividade -->
<!-- pureza -->
<div id="tab3"><ul><li><div class="item">
<div class="text-content">
<h4>Preciso da proteína totalmente purificada?</h4>
<span>Sobre a pureza da amostra</span>
<p>A porcentagem de pureza da amostra da proteína vai depender dos fins experimentais (Sciences,2010), veja aqui alguns exemplos:<br><ol>
<li><em>50% de pureza:</em> aceitável para a criação de um anticorpo monoclonal e para estudos cinéticos, desde que não contenha outras atividades competitivas (Sciences, 2016).</li>
<li><em>95% de pureza:</em> adequada para a análise de sequência de aminoácidos e caracterização físico-química, e cristalografia por raios X; porém inaceitável para criar um anticorpo policlonal monoespecífico, especialmente se os contaminantes forem altamente imunogênicos.</li>
<li><em>O maior nível de pureza:</em> necessário para proteínas terapêuticas.</li></ol></p>
<p>Conforme se avance com a purificação, será mais difícil remover os contaminantes residuais, além de que mais etapas implicam maior custo e tempo e diminuição do rendimento. Por isso, o recomendável é que se defina um nível aceitável de contaminantes e estudar a natureza dos mesmos para adotar a estratégia de purificação.</p>
</div></div></li></ul></div>
<!-- //pureza -->
<!-- fonte -->
<div id="tab4"><ul><li><div class="item">
<div class="text-content">
<h4>Qual fonte de proteínas devo utilizar?</h4>
<span>Fatores a considerar</span>
<p>Vai depender da disponibilidade da fonte, alto conteúdo da enzima, facilidade de extração de proteína se baixo conteúdo de interferentes que apresente; as fontes podem ser classificadas pela sua origem, elas apresentam vantagens e desvantagens:<br><ol>
<li><em>Plantas: </em>geralmente não são escolhidas como fonte de proteínas.</li>
<li><em>Bactéria ou Fungo:</em> eles podem ser cultivados sob condições definidas, e ainda podem permitira manipulação do nível de proteínas controlando o meio de cultura; porém pode possuir paredes celulares difíceis de quebrar.</li>
<li><em>Tecido animal</em>: se pretende isolar uma proteína específica de tecido, a melhor escolha é isolar a partir do tecido onde a fonte é mais abundante; mas se é mais fácil isolar a partir de outro que tem menor conteúdo, pode ser uma melhor aposta.</li></ol></p>
<p>Se a proteína de interesse está em quantidades muito pequenas ou somente encontrada em fontes inconvenientes, a clonagem e a expressão gênica são uma alternativa para a purificação.</p>
</div></div></li></ul></div>
<!-- /fonte -->
<!-- literatura -->
<div id="tab5"><ul><li><div class="item">
<div class="text-content">
<h4>Já foi isolada anteriormente?</h4>
<span>Revisão da literatura</span>
<p>É muito provável que a proteína de interesse ou outra relacionada tenham sido isoladas já e se encontrem na literatura. Portanto, é recomendável usar essas informações da literatura em vez de tentar reinventar a roda.</p>
</div></div></li></ul></div>
<!-- /literatura -->
</section></div></div>
</div>
<br><br><strong>Referências</strong><br><br>
<p>GE Healthcare Life Sciences. <a href="http://sevierlab.vet.cornell.edu/resources/Research-Links-Page/2-Molecular-Biology-and-Biochemisty-Resources/GE-Handbooks/GE_Protein_Sample_Preparation.pdf" target="_blank">Overview of protein sample preparation.</a> <em>In Protein Sample Preparation</em>, chapter 1, pages 13–26. 2016.</p>
<p>Shawn Doonan and Paul Cutler. <a href="http://link.springer.com/10.1385/1-59259-655-X:1" target="_blank">General Strategies</a>. <em>In Protein Purification Protocols</em>, chapter 1, pages 1–14. Humana Press, New Jersey, 2004. doi: 10.1385/1-59259-655-X:1.</p>
<p>Paul T Wingfield. <a href="https://doi.org/10.1002/0471140864.ps0601s80" target="_blank">Overview of the purification of recombinant proteins</a>. <em>Current Protocols in Protein Science</em>, 80(1):6.1.1–6.1.35, 2015.</p>
<p>Hui F Liu, Junfen Ma, Charles Winter, and Robert Bayer. <a href="https://doi.org/10.4161/mabs.2.5.12645" target="_blank">Recovery and purification process development for monoclonal antibody production</a>. <em>mAbs</em>, 2(5):480–499, 2010. doi: 10.4161/mabs.2.5.12645. PMID: 20647768.</p>
<p>BioProcess-Media. <a href="http://wolfson.huji.ac.il/purification/PDF/Others/AMERSHAM_ProteinPurificGuide.pdf" target="_blank">Protein and Peptide Purification – Technique selection guide</a>. Amersham Biosciences, AD edition, 2003.</p>
<p>Nikolaos E Labrou. <a href="https://doi.org/10.1007/978-1-0716-0775-6_1" target="_blank">Protein purification technologies</a>. <em>In Protein Downstream Processing</em>, chapter 1, pages 3–10. Humana Press, New York, 2020. ISBN 978-1-0716-0775-6. doi: 10.1007/978-1-0716-0775-6_1.</p>
<p>GE Healthcare Life Sciences. <a href="http://wolfson.huji.ac.il/purification/PDF/Others/GE_StratProtPurificHanbook.pdf" target="_blank">Purification examples</a>. <em>In Strategies for Protein Purification Handbook</em>, chapter 9, pages 109–124. 2010.</p>
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