{"id":4835,"date":"2015-06-27T15:40:00","date_gmt":"2015-06-27T19:40:00","guid":{"rendered":"https:\/\/www.med.unc.edu\/biochem\/directory\/carter\/"},"modified":"2025-08-13T08:14:33","modified_gmt":"2025-08-13T12:14:33","slug":"carter","status":"publish","type":"directory","link":"https:\/\/www.med.unc.edu\/biochem\/directory\/carter\/","title":{"rendered":"Charles Carter, Jr."},"content":{"rendered":"<p style=\"text-align: center\"><span class=\"blue\"><em><strong>Professor of Biochemistry and Biophysics<br \/>\n<\/strong><\/em><\/span><span class=\"discreet\">(PhD &#8211; University of California, San Diego)<\/span><\/p>\n<div>\n<h3><span class=\"blue\">HONORS &amp; AWARDS<\/span><\/h3>\n<ul>\n<li><span class=\"normalSizeFont\">Fellow, American Association for the Advancement of Science (AAAS) 2013<\/span><\/li>\n<li><span class=\"normalSizeFont\">American Institute of Physics Board of Directors, 2012-present<\/span><\/li>\n<\/ul>\n<h3>ACTIVE PROJECTS<\/h3>\n<p>Carter lab has funding from two Foundations for projects arising from interest in the <a href=\"https:\/\/carterlab.web.unc.edu\/research\/active-projects\/bitwise-evolution-of-the-genetic-code\/\">origin and evolution of the Genetic Code<\/a> <em>(Alfred P. <a href=\"https:\/\/news.unchealthcare.org\/2022\/02\/carter-awarded-1-5-million-for-origin-of-life-research\/\">Sloan<\/a> Foundation, $1.5 M)<\/em> and the emergence of <a href=\"https:\/\/carterlab.web.unc.edu\/research\/active-projects\/ribosome-free-codon-directed-peptide-bond-formation\/\">codon-directed protein synthesis<\/a> (<em>W. M. <a href=\"https:\/\/www.med.unc.edu\/biochem\/news\/carolina-scientists-earn-prestigious-keck-award\/\">Keck<\/a> Foundation, $1 M<\/em>) prior to the appearance of ribosomes.<\/p>\n<h3><span class=\"blue\"><span class=\"largeFont\">RESEARCH<\/span><\/span><\/h3>\n<p><em><span class=\"normalSizeFont\">Protein Crystallography, Structural Polymorphism and Function<\/span><\/em><\/p>\n<p style=\"text-align: justify\">The Carter lab uses structural, bioinformatic, molecular genetic, and biophysical techniques to strengthen and deepen understanding of the mechanistic basis and historical origins of enzyme catalysis.<a href=\"http:\/\/carterlab.web.unc.edu\/research\/\"> See also Carter lab website.<\/a><\/p>\n<p>Our structural biology research focuses on two problems:<\/p>\n<p><strong>How did the proteome emerge from pre-biotic chemistry?<\/strong><\/p>\n<p>Class I and II aminoacyl-tRNA synthetase superfamilies (aaRS). Translate the genetic code. Experimental properties of their deconstructed modules allow us to characterize development of catalysis from ~50 residue peptides. Multiple evidence argues that the two classes descended from opposite strands of a common ancestral gene. Unique information in that gene had two different, functional interpretations, depending on which strand is translated. The duality evokes visual puzzles ((Fig. 1; Martinez, et al. (2016); Carter, (2016)).<\/p>\n<p><img loading=\"lazy\" decoding=\"async\" class=\"alignnone size-medium wp-image-8576\" src=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-2-Hypercycle_duality-300x275.png\" alt=\"Pictures used to describe Figure 1. Dual genetic ancestry and catalytic interdependence of Class I and II aaRS\" width=\"300\" height=\"275\" srcset=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-2-Hypercycle_duality-300x275.png 300w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-2-Hypercycle_duality-768x704.png 768w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-2-Hypercycle_duality-1024x939.png 1024w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-2-Hypercycle_duality-558x512.png 558w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-2-Hypercycle_duality.png 1933w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><\/p>\n<p>Figure 1. Dual genetic ancestry and catalytic interdependence of Class I and II aaRS.<\/p>\n<p>Correlations between amino acid properties (Wolfenden), their exposed surface areas in folded proteins, and coding elements in transfer RNA clarify the \u201cchemical ecology\u201d of the Central Dogma (Fig. 2). Amino acid side chain behaviors determine folding of aaRS, giving them their reflexive ability to execute coding rules (curved arrow; Carter &amp; Wolfenden (2016)).<\/p>\n<p><img loading=\"lazy\" decoding=\"async\" class=\"alignnone size-medium wp-image-8575\" src=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-2-central_dogma_website-300x286.png\" alt=\"Picture used to describe Figure 2. Crick\u2019s Central Dogma and adaptor hypothesis in the ecology of amino acid phase transfer equilibria. \" width=\"300\" height=\"286\" srcset=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-2-central_dogma_website-300x286.png 300w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-2-central_dogma_website-768x731.png 768w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-2-central_dogma_website-1024x975.png 1024w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-2-central_dogma_website-538x512.png 538w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><\/p>\n<p>Figure 2. Crick\u2019s Central Dogma and adaptor hypothesis in the ecology of amino acid phase transfer equilibria.<\/p>\n<p><strong>How do long range intramolecular communications produce vectorial behavior in enzymes that transduce chemical free energy? <\/strong><\/p>\n<p>Catalytic conformational changes during tryptophan activation by Tryptophanyl-tRNA synthetase (TrpRS) become favorable only after release of PPi (Fig. 3, b,d; with Dokholyan group). Axes are conformational angles\u2014hinge bending and twisting\u2014accounting for 0.85 of the motion. Red spheres denoting the conformational transition states found by PATH program simulations match the saddle point of the free-energy surfaces. Unless the PPi leaving group dissociates, the equilibrium favors the pre-transition state at high twist. (See Carter, et al. (2017) Chandrasekaran &amp; Carter (2017).<\/p>\n<p><img loading=\"lazy\" decoding=\"async\" class=\"alignnone size-medium wp-image-8577\" src=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-3-DG_surfaces_1-11-16-300x268.png\" alt=\"4 graphs to describe Figure 3. Conformational Free energy landscapes depend on PPi product release.\" width=\"300\" height=\"268\" srcset=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-3-DG_surfaces_1-11-16-300x268.png 300w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-3-DG_surfaces_1-11-16-768x685.png 768w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-3-DG_surfaces_1-11-16-1024x914.png 1024w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-figure-3-DG_surfaces_1-11-16-574x512.png 574w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><\/p>\n<p>Figure 3. Conformational Free energy landscapes depend on PPi product release.<\/p>\n<p>High-order combinatorial permutation measures long-range coupling free energies responsible for catalysis and specificity. Experimental \u0394Gk<sub>cat<\/sub> values correlate with structural perturbations in 15 combinatorial mutations at 4 sites that impose the barrier between pre-transition and products states, and with parameters from computational trajectories. The correlations relate catalysis to structure directly and via the computed trajectories (see Chandrasekaran and Carter (2017).<\/p>\n<p><img loading=\"lazy\" decoding=\"async\" class=\"alignnone size-medium wp-image-8578\" src=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-Figure-4-Paths_Kinetics_stabilities-300x287.jpg\" alt=\"Figure to describe Figure 4. Structural changes correlate closely with experimental, computational parameters.\" width=\"300\" height=\"287\" srcset=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-Figure-4-Paths_Kinetics_stabilities-300x287.jpg 300w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-Figure-4-Paths_Kinetics_stabilities-768x735.jpg 768w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-Figure-4-Paths_Kinetics_stabilities-1024x980.jpg 1024w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-Figure-4-Paths_Kinetics_stabilities-535x512.jpg 535w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2015\/06\/Carter-lab-Figure-4-Paths_Kinetics_stabilities.jpg 1959w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><\/p>\n<p>Figure 4. Structural changes correlate closely with experimental, computational parameters.<\/p>\n<h3><span id=\"Selected_publications_by_topic\">PUBLICATIONS<\/span><\/h3>\n<p><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/sites\/myncbi\/charles.carter.1\/bibliography\/40754127\/public\/?sort=date&amp;direction=ascending\">complete listing of publications for Charlie W. Carter Jr<\/a><\/p>\n<div>\n<hr \/>\n<\/div>\n<h3><span class=\"blue\">Lab Contact:<\/span><\/h3>\n<div>Lab rooms: 3100 G-H Genetic Medicine<\/div>\n<div>Lab Phone: 919-966-6781<\/div>\n<div><a href=\"https:\/\/carterlab.web.unc.edu\/research\/\">Carter lab website<\/a><\/div>\n<\/div>\n","protected":false},"excerpt":{"rendered":"<p><!-- description --> <\/p>\n<p class='lead'>Research: Protein crystallography, structural polymorphism and function<\/p>\n","protected":false},"featured_media":8133,"template":"","meta":{"_acf_changed":false,"layout":"","cellInformation":"","apiCallInformation":"","_links_to":"","_links_to_target":""},"class_list":["post-4835","directory","type-directory","status-publish","has-post-thumbnail","hentry","odd"],"acf":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.8 - https:\/\/yoast.com\/product\/yoast-seo-wordpress\/ -->\n<title>Charles Carter, Jr. | Biochemistry and Biophysics<\/title>\n<meta name=\"description\" content=\"Charlie 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