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Previous random" /> <meta name="robots" content="noindex" /> <title>Libraries of random-sequence polypeptides produced with high yield as carboxy-terminal fusions with ubiquitin | Stuart Kauffman - Academia.edu</title> <link rel="canonical" href="https://www.academia.edu/110296444/Libraries_of_random_sequence_polypeptides_produced_with_high_yield_as_carboxy_terminal_fusions_with_ubiquitin" /> <script async src="https://www.googletagmanager.com/gtag/js?id=G-5VKX33P2DS"></script> <script> window.dataLayer = window.dataLayer || []; function gtag(){dataLayer.push(arguments);} gtag('js', new Date()); gtag('config', 'G-5VKX33P2DS', { cookie_domain: 'academia.edu', send_page_view: false, }); gtag('event', 'page_view', { 'controller': "single_work", 'action': "show", 'controller_action': 'single_work#show', 'logged_in': 'false', 'edge': 'unknown', // Send nil if there is no A/B test bucket, in case some records get logged // with missing data - that way we can distinguish between the two cases. // ab_test_bucket should be of the form <ab_test_name>:<bucket> 'ab_test_bucket': null, }) </script> <script> var $controller_name = 'single_work'; var $action_name = "show"; var $rails_env = 'production'; var $app_rev = '49879c2402910372f4abc62630a427bbe033d190'; var $domain = 'academia.edu'; var $app_host = "academia.edu"; var $asset_host = "academia-assets.com"; var $start_time = new Date().getTime(); var $recaptcha_key = "6LdxlRMTAAAAADnu_zyLhLg0YF9uACwz78shpjJB"; var $recaptcha_invisible_key = "6Lf3KHUUAAAAACggoMpmGJdQDtiyrjVlvGJ6BbAj"; var $disableClientRecordHit = false; </script> <script> window.require = { config: function() { return function() {} } } </script> <script> window.Aedu = window.Aedu || {}; window.Aedu.hit_data = null; window.Aedu.serverRenderTime = new Date(1732410737000); window.Aedu.timeDifference = new Date().getTime() - 1732410737000; </script> <script type="application/ld+json">{"@context":"https://schema.org","@type":"ScholarlyArticle","abstract":"Libraries of random-sequence polypeptides have been shown to be valuable sources of novel molecules possessing a variety of useful biologic-like activities, some of which may hold promise as potential vaccines and therapeutics. Previous random peptide expression systems were limited to low levels of peptide production and often to short sequences. Here we describe a series of libraries designed for increased polypeptide length. Cloned as carboxy-terminal extensions of ubiquitin, the fusions were produced in E. coli at high levels, and were purified to homogeneity. The majority of the extension proteins examined could be cleaved from ubiquitin by treatment with a ubiquitin-fusion hydrolase. The libraries described here are appropriate sources of novel polypeptides with desired binding or catalytic function, as well as tools with which to examine inherent properties of proteins as a whole. Toward the latter goal, we have examined structural properties of random-sequence proteins purified from these libraries. Quite surprisingly, fluorescence emission spectra of intrinsic tryptophan residues in several purified fusion proteins, under native-like and denaturing conditions, often resemble those expected for folded and unfolded states, respectively. The results presented here detail an important expansion in the range of potential uses for random-sequence polypeptide libraries.","author":[{"@context":"https://schema.org","@type":"Person","name":"Stuart Kauffman"}],"contributor":[],"dateCreated":"2023-12-01","dateModified":null,"datePublished":"1995-01-01","headline":"Libraries of random-sequence polypeptides produced with high yield as carboxy-terminal fusions with ubiquitin","inLanguage":"en","keywords":["Computational Biology","Biology","Medicine","Ubiquitin","Escherichia coli","Molecular Diversity","Peptides","Peptide","Library Design","Molecular cloning","Amino Acids","Structural Properties","Base Sequence","Fusion Protein"],"locationCreated":null,"publication":"Molecular Diversity","publisher":{"@context":"https://schema.org","@type":"Organization","name":null},"image":null,"thumbnailUrl":null,"url":"https://www.academia.edu/110296444/Libraries_of_random_sequence_polypeptides_produced_with_high_yield_as_carboxy_terminal_fusions_with_ubiquitin","sourceOrganization":[{"@context":"https://schema.org","@type":"EducationalOrganization","name":null}]}</script><link rel="stylesheet" media="all" href="//a.academia-assets.com/assets/single_work_page/loswp-352e32ba4e89304dc0b4fa5b3952eef2198174c54cdb79066bc62e91c68a1a91.css" /><link rel="stylesheet" media="all" href="//a.academia-assets.com/assets/design_system/body-8d679e925718b5e8e4b18e9a4fab37f7eaa99e43386459376559080ac8f2856a.css" /><link rel="stylesheet" media="all" href="//a.academia-assets.com/assets/design_system/heading-b2b823dd904da60a48fd1bfa1defd840610c2ff414d3f39ed3af46277ab8df3b.css" /><link crossorigin="" href="https://fonts.gstatic.com/" rel="preconnect" /><link 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window.loswp.shouldShowBulkDownload = true; window.loswp.showSignupCaptcha = false window.loswp.willEdgeCache = false; window.loswp.work = {"work":{"id":110296444,"created_at":"2023-12-01T06:37:35.173-08:00","from_world_paper_id":244506315,"updated_at":"2023-12-01T07:01:02.191-08:00","_data":{"abstract":"Libraries of random-sequence polypeptides have been shown to be valuable sources of novel molecules possessing a variety of useful biologic-like activities, some of which may hold promise as potential vaccines and therapeutics. Previous random peptide expression systems were limited to low levels of peptide production and often to short sequences. Here we describe a series of libraries designed for increased polypeptide length. Cloned as carboxy-terminal extensions of ubiquitin, the fusions were produced in E. coli at high levels, and were purified to homogeneity. The majority of the extension proteins examined could be cleaved from ubiquitin by treatment with a ubiquitin-fusion hydrolase. The libraries described here are appropriate sources of novel polypeptides with desired binding or catalytic function, as well as tools with which to examine inherent properties of proteins as a whole. Toward the latter goal, we have examined structural properties of random-sequence proteins purified from these libraries. Quite surprisingly, fluorescence emission spectra of intrinsic tryptophan residues in several purified fusion proteins, under native-like and denaturing conditions, often resemble those expected for folded and unfolded states, respectively. The results presented here detail an important expansion in the range of potential uses for random-sequence polypeptide libraries.","publication_date":"1995,,","publication_name":"Molecular Diversity"},"document_type":"paper","pre_hit_view_count_baseline":null,"quality":null,"language":"en","title":"Libraries of random-sequence polypeptides produced with high yield as carboxy-terminal fusions with ubiquitin","broadcastable":false,"draft":null,"has_indexable_attachment":null,"indexable":true}}["work"]; window.loswp.workCoauthors = [38651941]; window.loswp.locale = "en"; window.loswp.countryCode = "SG"; window.loswp.cwvAbTestBucket = ""; window.loswp.designVariant = "grid"; window.loswp.fullPageMobileSutdModalVariant = "control"; window.loswp.useOptimizedScribd4genScript = false; window.loswp.appleClientId = 'edu.academia.applesignon';</script><script defer="" src="https://accounts.google.com/gsi/client"></script><div class="loswp-grid--container"><div data-auto_select="false" data-client_id="331998490334-rsn3chp12mbkiqhl6e7lu2q0mlbu0f1b" data-landing_url="https://www.academia.edu/110296444/Libraries_of_random_sequence_polypeptides_produced_with_high_yield_as_carboxy_terminal_fusions_with_ubiquitin" data-login_uri="https://www.academia.edu/registrations/google_one_tap" data-moment_callback="onGoogleOneTapEvent" id="g_id_onload"></div><div class="above-fold js-swp-splash-above-fold"><div class="work-card--container js-swp-control-work-card" data-entity-id="110296444"><div class="work-cover--wrapper"><div class="work-cover--container"><div class="work-cover--no-attachment-container js-swp-splash-paper-cover"><div class="work-cover--file-icon-wrapper"><img alt="paper cover icon" src="//a.academia-assets.com/images/single_work_splash/adobe.icon.svg" /></div><div class="work-cover--title js-swp-splash-paper-cover-page-title">Libraries of random-sequence polypeptides produced with high yield as carboxy-terminal fusions with ubiquitin</div><br /><div style="margin-top: 170px"><button class="work-cover--request-pdf-button js-request-pdf-button"><svg style="width: 14px; margin-right: 8px;" aria-hidden="true" focusable="false" data-prefix="fas" data-icon="envelope" class="svg-inline--fa fa-envelope fa-w-16" role="img" xmlns="http://www.w3.org/2000/svg" viewBox="0 0 512 512"><path fill="currentColor" d="M502.3 190.8c3.9-3.1 9.7-.2 9.7 4.7V400c0 26.5-21.5 48-48 48H48c-26.5 0-48-21.5-48-48V195.6c0-5 5.7-7.8 9.7-4.7 22.4 17.4 52.1 39.5 154.1 113.6 21.1 15.4 56.7 47.8 92.2 47.6 35.7.3 72-32.8 92.3-47.6 102-74.1 131.6-96.3 154-113.7zM256 320c23.2.4 56.6-29.2 73.4-41.4 132.7-96.3 142.8-104.7 173.4-128.7 5.8-4.5 9.2-11.5 9.2-18.9v-19c0-26.5-21.5-48-48-48H48C21.5 64 0 85.5 0 112v19c0 7.4 3.4 14.3 9.2 18.9 30.6 23.9 40.7 32.4 173.4 128.7 16.8 12.2 50.2 41.8 73.4 41.4z"></path></svg>Request PDF</button></div></div></div></div><div class="work-card--content"><h1 class="work-card--title">Libraries of random-sequence polypeptides produced with high yield as carboxy-terminal fusions with ubiquitin</h1><div class="work-card--pub-info">Molecular Diversity, 1995</div><a class="js-profile-link work-card--single-author" data-has-card-for-user="38651941" href="https://independent.academia.edu/StuartKauffman?swp=tc-au-110296444"><div class="work-card--single-author-photo"><img class="Avatar--circle s65 Avatar--xxxs" shape="circle" border="0" alt="" src="//a.academia-assets.com/images/s65_no_pic.png" /></div><div class="work-card--author-name-wrapper" style="max-width: 125px; font-weight: 500; color: #4b4b4b;"><div class="u-textTruncate"><span itemprop="author">Stuart Kauffman</span></div></div></a><script data-card-contents-for-user="38651941" type="text/json">{"id":38651941,"first_name":"Stuart","middle_initials":null,"last_name":"Kauffman","page_name":"StuartKauffman","domain_name":"independent","created_at":"2015-11-18T13:57:30.814-08:00","display_name":"Stuart Kauffman","url":"https://independent.academia.edu/StuartKauffman","photo":"/images/s65_no_pic.png","has_photo":false,"interests":[{"id":6018,"name":"Markets","url":"https://www.academia.edu/Documents/in/Markets"},{"id":1074,"name":"Organizational Theory","url":"https://www.academia.edu/Documents/in/Organizational_Theory"},{"id":209,"name":"Social Theory","url":"https://www.academia.edu/Documents/in/Social_Theory"},{"id":46271,"name":"Strategy","url":"https://www.academia.edu/Documents/in/Strategy"},{"id":21168,"name":"Strategy (Business)","url":"https://www.academia.edu/Documents/in/Strategy_Business_"}]}</script><div class="work-card--no-attachment-details"><div style="font-weight: 700; font-size: 14px;">Abstract</div><div class="work-card--abstract js-swp-splash-abstract">Libraries of random-sequence polypeptides have been shown to be valuable sources of novel molecules possessing a variety of useful biologic-like activities, some of which may hold promise as potential vaccines and therapeutics. Previous random peptide expression systems were limited to low levels of peptide production and often to short sequences. Here we describe a series of libraries designed for increased polypeptide length. Cloned as carboxy-terminal extensions of ubiquitin, the fusions were produced in E. coli at high levels, and were purified to homogeneity. The majority of the extension proteins examined could be cleaved from ubiquitin by treatment with a ubiquitin-fusion hydrolase. The libraries described here are appropriate sources of novel polypeptides with desired binding or catalytic function, as well as tools with which to examine inherent properties of proteins as a whole. Toward the latter goal, we have examined structural properties of random-sequence proteins purified from these libraries. Quite surprisingly, fluorescence emission spectra of intrinsic tryptophan residues in several purified fusion proteins, under native-like and denaturing conditions, often resemble those expected for folded and unfolded states, respectively. The results presented here detail an important expansion in the range of potential uses for random-sequence polypeptide libraries.</div></div><div class="request-upload--container"><p class="request-upload--title">Stuart Kauffman hasn't uploaded this paper.</p><div class="request-upload--info-text"><svg aria-hidden="true" focusable="false" data-prefix="fas" data-icon="info-circle" class="request-upload--info-icon svg-inline--fa fa-info-circle fa-w-16" role="img" xmlns="http://www.w3.org/2000/svg" viewBox="0 0 512 512"><path fill="currentColor" d="M256 8C119.043 8 8 119.083 8 256c0 136.997 111.043 248 248 248s248-111.003 248-248C504 119.083 392.957 8 256 8zm0 110c23.196 0 42 18.804 42 42s-18.804 42-42 42-42-18.804-42-42 18.804-42 42-42zm56 254c0 6.627-5.373 12-12 12h-88c-6.627 0-12-5.373-12-12v-24c0-6.627 5.373-12 12-12h12v-64h-12c-6.627 0-12-5.373-12-12v-24c0-6.627 5.373-12 12-12h64c6.627 0 12 5.373 12 12v100h12c6.627 0 12 5.373 12 12v24z"></path></svg><p class="no-margin hide-on-small-mobile">Let Stuart know you want this paper to be uploaded.</p><p class="no-margin hide-above-small-mobile">Ask for this paper to be uploaded.</p></div><button class="work-cover--request-pdf-button small js-request-pdf-button hide-on-desktop"><svg style="width: 14px; 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