{"id":95,"date":"2024-12-09T10:37:48","date_gmt":"2024-12-09T15:37:48","guid":{"rendered":"https:\/\/www.golive.clarku.edu\/faculty\/profiles\/shuanghong-huo\/"},"modified":"2026-04-05T07:34:30","modified_gmt":"2026-04-05T11:34:30","slug":"shuanghong-huo","status":"publish","type":"cu_faculty","link":"https:\/\/www.clarku.edu\/faculty\/profiles\/shuanghong-huo\/","title":{"rendered":"Shuanghong Huo"},"content":{"rendered":"<p style=\"text-align:justify\">Sharon Huo graduated from Peking University in 1990, majoring in Applied Chemistry. After working at the Institute of Chemistry, Chinese Academy of Sciences for four years, she started her Ph.D. study at Boston University, followed by post-doctoral training at UC-San Francisco. She joined the faculty of Clark University in 2001 as a tenure-track Assistant Professor and was promoted to full professor in 2015. Her research is in the field of computational biophysics. She studies the allosteric effect in proteins, protein folding\/misfolding\/aggregation, and protein-ligand interaction using computational approaches. Her research was supported by NIH, NSF, and private agents. She has established herself in the field of studying amyloidogenic proteins. In recent years, one of her research foci has been to develop analysis methods to extract kinetic information from molecular dynamics simulations. The methods developed in her group include the MaxFlux reaction-path algorithm combined with the probabilistic roadmap motion planning method, graph representation of protein free energy landscape, and diffusion maps with a hybrid\u00a0geometry energy-based kernel. Currently, her group is using graph theory and information theory to study allosteric proteins.\u00a0<br \/>Group website:\u00a0<a href=\"https:\/\/wordpress.clarku.edu\/shuo\/\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/wordpress.clarku.edu\/shuo\/<\/a><br \/><strong><br \/>Selected peer-reviewed publications:<\/strong><\/p>\n<p>Yang, T., Han, L., and\u00a0Huo, S.\u00a0(2022) Dynamics and Allosteric Information Pathways of Unphosphorylated c<strong>\u2011<\/strong>Cbl,\u00a0<em><strong>J. Chem. Inf. Model.<\/strong><\/em>\u00a062, 6148.\u00a0<\/p>\n<p>Tan, Q., Liu, H., Duan, M.,<sup> <\/sup>and Huo, S. (2021) Interplay between Human Islet Amyloid Polypeptide Aggregates and Micro-heterogeneous Membranes, <strong><em>BBA &#8211; Biomembranes<\/em><\/strong> 1863, 183691.<\/p>\n<p>Tan, Q., Duan, M,. Li, M., Han, Li., and Huo, S. (2019) Approximating dynamic proximity with a hybrid geometry energy-based kernel for diffusion maps. <em><strong>J. Chem. Phys. <\/strong>151, 105101<\/em><span>.<\/span><\/p>\n<p>Duan, M., Liu, H., Li, M., and Huo, S. (2015) Network representation of conformational transitions between hidden intermediates of Rd-apocytochrome <em>b562<\/em>. <strong><em>J. Chem. Phys. <\/em><\/strong>143, 135101.<span>\u00a0<\/span><\/p>\n<p><span>Li, M., Duan, M., Fan, J., Han, L., and <\/span><span>Huo, S. <\/span><span>(2013) Graph representation of protein<\/span> <span>free energy \u00a0\u00a0landscape. <\/span><em><strong>J. Chem. Phys. <\/strong><\/em><span>139: 185101.<\/span><\/p>\n","protected":false},"author":0,"featured_media":1901,"parent":0,"template":"","meta":{"cu_faculty_f180_userid":"C14761355","cu_faculty_first_name":"Shuanghong","cu_faculty_last_name":"Huo","cu_faculty_employment_status":"Full Time","cu_faculty_rank":"Professor","cu_faculty_position":"Professor","cu_faculty_phone":"","cu_faculty_email":"shuo@clarku.edu","cu_faculty_location":"","cu_faculty_about":"<p style=\"text-align:justify;\">Sharon Huo graduated from Peking University in 1990, majoring in Applied Chemistry. After working at the Institute of Chemistry, Chinese Academy of Sciences for four years, she started her Ph.D. study at Boston University, followed by post-doctoral training at UC-San Francisco. She joined the faculty of Clark University in 2001 as a tenure-track Assistant Professor and was promoted to full professor in 2015. Her research is in the field of computational biophysics. She studies the allosteric effect in proteins, protein folding\/misfolding\/aggregation, and protein-ligand interaction using computational approaches. Her research was supported by NIH, NSF, and private agents. She has established herself in the field of studying amyloidogenic proteins. In recent years, one of her research foci has been to develop analysis methods to extract kinetic information from molecular dynamics simulations. The methods developed in her group include the MaxFlux reaction-path algorithm combined with the probabilistic roadmap motion planning method, graph representation of protein free energy landscape, and diffusion maps with a hybrid\u00a0geometry energy-based kernel. Currently, her group is using graph theory and information theory to study allosteric proteins.\u00a0<br>Group website:\u00a0<a href=\"https:\/\/wordpress.clarku.edu\/shuo\/\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/wordpress.clarku.edu\/shuo\/<\/a><br><strong><br>Selected peer-reviewed publications:<\/strong><\/p>\n<p>Yang, T., Han, L., and\u00a0Huo, S.\u00a0(2022) Dynamics and Allosteric Information Pathways of Unphosphorylated c<strong>\u2011<\/strong>Cbl,\u00a0<em><strong>J. Chem. Inf. Model.<\/strong><\/em>\u00a062, 6148.\u00a0<\/p>\n<p>Tan, Q., Liu, H., Duan, M.,<sup> <\/sup>and Huo, S. (2021) Interplay between Human Islet Amyloid Polypeptide Aggregates and Micro-heterogeneous Membranes, <strong><em>BBA - Biomembranes<\/em><\/strong> 1863, 183691.<\/p>\n<p>Tan, Q., Duan, M,. Li, M., Han, Li., and Huo, S. (2019) Approximating dynamic proximity with a hybrid geometry energy-based kernel for diffusion maps. <em><strong>J. Chem. Phys. <\/strong>151, 105101<\/em><span>.<\/span><\/p>\n<p>Duan, M., Liu, H., Li, M., and Huo, S. (2015) Network representation of conformational transitions between hidden intermediates of Rd-apocytochrome <em>b562<\/em>. <strong><em>J. Chem. Phys. <\/em><\/strong>143, 135101.<span>\u00a0<\/span><\/p>\n<p><span>Li, M., Duan, M., Fan, J., Han, L., and <\/span><span>Huo, S. <\/span><span>(2013) Graph representation of protein<\/span> <span>free energy \u00a0\u00a0landscape. <\/span><em><strong>J. Chem. Phys. <\/strong><\/em><span>139: 185101.<\/span><\/p>","cu_faculty_degrees":"<span>Ph.D. in Computational Chemistry,<\/span> Boston University, 1999\n<span>B.S. in Chemistry,<\/span> Peking University, 1990","cu_faculty_cv":"https:\/\/faculty180.interfolio.com\/public\/download.php?key=SDRwNCtxSUpsamxBQ213WS9ucHFuNnMwT0hzQU11b2RPQkJ2cWc3amxyUmNRdVVXTkF4MU11R2dYUnVFTGs0STdpK05TNW9pVWE1VHYvVzB0UldFUlVTM2pMNXhHSVU3T0pWSTJlTlNJVTg9","cu_faculty_links":"[]","cu_faculty_scholarly_interests":"Computational Biophysics","cu_faculty_scholarly_works":"[{\"activityid\":13835,\"fields\":{\"Type\":\"Articles in Refereed Journals\",\"Title\":\"The disordered negatively charged C-terminus of the large HECT E3 ubiquitin ligase HERC2 provides structural and thermal stability to the HECT C-lobe\",\"Journal Title\":\"Protein science : a publication of the Protein Society\",\"Series Title\":null,\"Month \\\/ Season\":null,\"Year\":2024,\"Publisher\":null,\"Publisher City and State\":null,\"Publisher Country\":null,\"Volume\":\"33\",\"Issue Number \\\/ Edition\":\"12\",\"Page Number(s) or Number of Pages\":\"e5229\",\"ISSN\":null,\"DOI\":null,\"CoAuthor\":null,\"URL\":null,\"Description\":\"Homologous to the C-terminus of E6AP (HECT) and RCC1-like domain (RLD)-containing protein 2 (HERC2) is a large, 528\\u2009kDa E3 ubiquitin ligase that is associated with cancer, oculocutaneous albanism type 2, Prader-Willi syndrome, and other neurological diseases. HERC2 has been found to contribute to double-stranded DNA break repairs, tumor suppression, maintaining centrosome architecture, and ubiquitylation. The C-terminal portion of the HECT domain (C-lobe) of HERC2 is responsible for transferring ubiquitin to a substrate but the precise function of the other eight domains in HERC2 are unknown. Interestingly, HERC2 contains a unique and negatively charged C-terminal tail adjoined to the C-lobe that is predicted to act as a linker to promote interactions between HERC2 and its binding partners. This study aims to better understand the function and relevance of HERC2 in disease by investigating the structural aspects of the HERC2 C-lobe and HERC2 C-terminal tail using AlphaFold followed by molecular dynamics (MD) simulations, multidimensional nuclear magnetic resonance (NMR), and circular dichroism (CD). Secondary structure content analysis from MD simulations and the fully resonance assigned H-N HSQC spectra of the HERC2 C-lobe and the isolated C-terminal tail confirm that the C-lobe is well-folded but the C-terminal tail is disordered. CD melting curves indicate that the flexible C-terminal tail provides improved stability to the C-lobe. Additionally, MD simulations have identified that the interaction between residues D4829 and R4728 is prevalent among the non-bonded contacts between the tail and the C-lobe. Overall, our results demonstrate that the negatively charged C-terminal tail is disordered, provides stability to the C-lobe, and may act as a flexible scaffold for protein-protein interactions.\",\"Include description in output citation\":0,\"Origin\":\"PubMed\"},\"facultyid\":\"C14761355\",\"status\":[{\"id\":13835,\"status\":\"Completed\\\/Published\",\"term\":\"Fall\",\"year\":2024,\"termid\":\"2024\\\/01\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C14761355\",\"attachments\":[],\"coauthors_list\":[\"Kelly  L Waters\",\"Kayla  J Rich\",\"Noah  D Schwaegerle\",\"Tianyi Yang\",\"Shuanghong Huo\",\"Donald  E Spratt\"],\"sort_date\":\"2024-9-01\"},{\"activityid\":10900,\"fields\":{\"Type\":\"Articles in Refereed Journals\",\"Title\":\"&lt;span style=&quot;font-size:12pt;color:#444444;&quot;&gt;Dynamics and Allosteric Information Pathways of Unphosphorylated c&lt;strong&gt;\\u2011&lt;\\\/strong&gt;Cbl&lt;\\\/span&gt;\",\"Journal Title\":\"J. Chem. Inf. Model.\",\"Series Title\":\"\",\"Month \\\/ Season\":\"\",\"Year\":2022,\"Publisher\":\"American Chemical Society\",\"Publisher City and State\":\"\",\"Publisher Country\":\"\",\"Volume\":\"62\",\"Issue Number \\\/ Edition\":\"\",\"Page Number(s) or Number of Pages\":\"6148\\u22126159\",\"ISSN\":\"\",\"DOI\":\"https:\\\/\\\/doi.org\\\/10.1021\\\/acs.jcim.2c01022\",\"CoAuthor\":null,\"URL\":\"\",\"Description\":\"\",\"Include description in output citation\":0,\"Origin\":\"Manual\"},\"facultyid\":\"C14761355\",\"status\":[{\"id\":10900,\"status\":\"Completed\\\/Published\",\"term\":\"Fall\",\"year\":2022,\"termid\":\"2022\\\/01\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C14761355\",\"attachments\":[],\"coauthors_list\":[\"Tianyi Yang\",\"Li Han\",\"Shuanghong Huo\"],\"sort_date\":\"2022-9-01\"},{\"activityid\":7030,\"fields\":{\"Type\":\"Presentations\",\"Title of Presentation\":\"Allosteric signal propagation pathways of unphosphorylated RING-type E3 ubiquitin ligase c-Cbl\",\"Conference \\\/ Meeting Name\":\"ACS (American Chemical Society) Annual Meeting, Fall 2022\",\"Location of Conference \\\/ Meeting\":\"Chicago, IL\",\"Month \\\/ Season\":\"August\",\"Year\":2022,\"Sponsoring Organization\":\"ACS\",\"CoAuthor\":null,\"URL\":\"\",\"Description\":\"\",\"Include description in output citation\":0,\"Origin\":\"Manual\"},\"facultyid\":\"C14761355\",\"status\":[{\"id\":7030,\"status\":\"Accepted\",\"term\":\"Summer\",\"year\":2024,\"termid\":\"2023\\\/05\",\"listingorder\":4,\"completionorder\":4},{\"id\":7030,\"status\":\"Accepted\",\"term\":\"Summer\",\"year\":2023,\"termid\":\"2022\\\/05\",\"listingorder\":4,\"completionorder\":4},{\"id\":7030,\"status\":\"Accepted\",\"term\":\"Spring\",\"year\":2022,\"termid\":\"2021\\\/03\",\"listingorder\":4,\"completionorder\":4}],\"userid\":\"C14761355\",\"attachments\":[],\"coauthors_list\":[\"Tianyi Yang\",\"Li Han\",\"Shuanghong Huo\"],\"sort_date\":\"2022-8-01\"},{\"activityid\":6084,\"fields\":{\"Type\":\"Articles in Refereed Journals\",\"Title\":\"Contrasting solution-state properties within a family of amyloidbinding molecular tools\",\"Journal Title\":\"Tetrahedron\",\"Series Title\":\"\",\"Month \\\/ Season\":\"\",\"Year\":2022,\"Publisher\":\"Elsevier\",\"Publisher City and State\":\"Amsterdam\",\"Publisher Country\":\"Netherlands\",\"Volume\":\"\",\"Issue Number \\\/ Edition\":\"\",\"Page Number(s) or Number of Pages\":\"\",\"ISSN\":\"\",\"DOI\":\"https:\\\/\\\/doi.org\\\/10.1016\\\/j.tet.2022.132817\",\"CoAuthor\":null,\"URL\":\"\",\"Description\":\"\",\"Include description in output citation\":0,\"Origin\":\"Manual\"},\"facultyid\":\"C14761355\",\"status\":[{\"id\":6084,\"status\":\"Completed\\\/Published\",\"term\":\"Spring\",\"year\":2022,\"termid\":\"2021\\\/03\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C14761355\",\"attachments\":[],\"coauthors_list\":[\"Anh-Vy Le\",\"Muyun Xu\",\"Tianyi Yang\",\"Luke Barrows\",\"Devon F. A. Fontaine\",\"Shuanghong Huo\",\"Charles Jakobsche\"],\"sort_date\":\"2022-1-01\"},{\"activityid\":4348,\"fields\":{\"Type\":\"Articles in Refereed Journals\",\"Title\":\"Interplay between Human Islet Amyloid Polypeptide Aggregates and Microhetergeneous Membranes\",\"Journal Title\":\"BBA-Biomembrane\",\"Series Title\":\"\",\"Month \\\/ Season\":\"\",\"Year\":2021,\"Publisher\":\"Elsevier\",\"Publisher City and State\":\" Amsterdam\",\"Publisher Country\":\"Netherlands\",\"Volume\":\"\",\"Issue Number \\\/ Edition\":\"\",\"Page Number(s) or Number of Pages\":\"\",\"ISSN\":\"\",\"DOI\":\"\",\"CoAuthor\":null,\"URL\":\"https:\\\/\\\/doi.org\\\/10.1016\\\/j.bbamem.2021.183691\",\"Description\":\"\",\"Include description in output citation\":0,\"Origin\":\"Manual\"},\"facultyid\":\"C14761355\",\"status\":[{\"id\":4348,\"status\":\"Completed\\\/Published\",\"term\":\"Fall\",\"year\":2021,\"termid\":\"2021\\\/01\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C14761355\",\"attachments\":[{\"attachmentid\":4502,\"mimetype\":\"application\\\/pdf\",\"filename\":\"BBA_qtan_2021.pdf\",\"filesize\":5127145,\"downloadurl\":\"https:\\\/\\\/faculty180.interfolio.com\\\/public\\\/download.php?key=SDRwNCtxSUpsamxBQ213WS9ucHFuNnMwT0hzQU11b2RPQkJ2cWc3amxyUmNRdVVXTkF4MU11R2dYUnVFTGs0SXp6d1lCV0hwUHRnQW5XaThTZ3d1bWhvRUE1V2tQdHJHeVNOSEduOC82bDE4c1UzNWVONWJhZz09\"}],\"coauthors_list\":[\"Qingzhe Tan\",\"Hanzhong Liu\",\"Mojie Duan\",\"Shuanghong Huo\"],\"sort_date\":\"2021-9-01\"},{\"activityid\":1764,\"fields\":{\"Type\":\"Articles in Refereed Journals\",\"Title\":\"Approximating dynamic proximity with a hybrid geometry energy-based kernel for diffusion maps\",\"Journal Title\":\"The Journal of chemical physics\",\"Series Title\":null,\"Month \\\/ Season\":null,\"Year\":2019,\"Publisher\":null,\"Publisher City and State\":null,\"Publisher Country\":null,\"Volume\":\"151\",\"Issue Number \\\/ Edition\":\"10\",\"Page Number(s) or Number of Pages\":\"105101\",\"ISSN\":null,\"DOI\":null,\"CoAuthor\":null,\"URL\":null,\"Description\":\"The diffusion map is a dimensionality reduction method. The reduction coordinates are associated with the leading eigenfunctions of the backward Fokker-Planck operator, providing a dynamic meaning for these coordinates. One of the key factors that affect the accuracy of diffusion map embedding is the dynamic measure implemented in the Gaussian kernel. A common practice in diffusion map study of molecular systems is to approximate dynamic proximity with RMSD (root-mean-square deviation). In this paper, we present a hybrid geometry-energy based kernel. Since high energy-barriers may exist between geometrically similar conformations, taking both RMSD and energy difference into account in the kernel can better describe conformational transitions between neighboring conformations and lead to accurate embedding. We applied our diffusion map method to the \\u03b2-hairpin of the B1 domain of streptococcal protein G and to Trp-cage. Our results in \\u03b2-hairpin show that the diffusion map embedding achieves better results with the hybrid kernel than that with the RMSD-based kernel in terms of free energy landscape characterization and a new correlation measure between the cluster center Euclidean distances in the reduced-dimension space and the reciprocals of the total net flow between these clusters. In addition, our diffusion map analysis of the ultralong molecular dynamics trajectory of Trp-cage has provided a unified view of its folding mechanism. These promising results demonstrate the effectiveness of our diffusion map approach in the analysis of the dynamics and thermodynamics of molecular systems. The hybrid geometry-energy criterion could be also useful as a general dynamic measure for other purposes.\",\"Include description in output citation\":0,\"Origin\":\"PubMed\"},\"facultyid\":\"C14761355\",\"status\":[{\"id\":1764,\"status\":\"Completed\\\/Published\",\"term\":\"Fall\",\"year\":2019,\"termid\":\"2019\\\/01\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C14761355\",\"attachments\":[],\"coauthors_list\":[\"Qingzhe Tan\",\"Mojie Duan\",\"Minghai Li\",\"Li Han\",\"Shuanghong Huo\"],\"sort_date\":\"2019-9-01\"}]","cu_faculty_awards_and_grants":"","cu_faculty_title":"Professor, Chemistry","cu_faculty_department":"Chemistry","cu_faculty_affiliated_departments":"Chemistry","footnotes":""},"cu_faculty_group":[],"cu_faculty_department":[24],"cu_faculty_position":[],"class_list":["post-95","cu_faculty","type-cu_faculty","status-publish","has-post-thumbnail","hentry","cu_faculty_department-chemistry"],"yoast_head":"<!-- This site is optimized with the Yoast SEO Premium plugin v27.2 (Yoast SEO v27.3) - https:\/\/yoast.com\/product\/yoast-seo-premium-wordpress\/ -->\n<title>Shuanghong Huo | Faculty<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.clarku.edu\/faculty\/profiles\/shuanghong-huo\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Shuanghong Huo\" \/>\n<meta property=\"og:description\" content=\"Sharon Huo graduated from Peking University in 1990, majoring in Applied Chemistry. After working at the Institute of Chemistry, Chinese Academy of Sciences for four years, she started her Ph.D. study at Boston University, followed by post-doctoral training at UC-San Francisco. She joined the faculty of Clark University in 2001 as a tenure-track Assistant Professor [&hellip;]\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.clarku.edu\/faculty\/profiles\/shuanghong-huo\/\" \/>\n<meta property=\"og:site_name\" content=\"Faculty\" \/>\n<meta property=\"article:modified_time\" content=\"2026-04-05T11:34:30+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/www.clarku.edu\/faculty\/wp-content\/uploads\/sites\/5\/2024\/12\/Shuanghong-Huo-720x720-1.jpg\" \/>\n\t<meta property=\"og:image:width\" content=\"720\" \/>\n\t<meta property=\"og:image:height\" content=\"720\" \/>\n\t<meta property=\"og:image:type\" content=\"image\/jpeg\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:label1\" content=\"Est. reading time\" \/>\n\t<meta name=\"twitter:data1\" content=\"2 minutes\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\\\/\\\/schema.org\",\"@graph\":[{\"@type\":\"WebPage\",\"@id\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/profiles\\\/shuanghong-huo\\\/\",\"url\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/profiles\\\/shuanghong-huo\\\/\",\"name\":\"Shuanghong Huo | Faculty\",\"isPartOf\":{\"@id\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/#website\"},\"primaryImageOfPage\":{\"@id\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/profiles\\\/shuanghong-huo\\\/#primaryimage\"},\"image\":{\"@id\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/profiles\\\/shuanghong-huo\\\/#primaryimage\"},\"thumbnailUrl\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/wp-content\\\/uploads\\\/sites\\\/5\\\/2024\\\/12\\\/Shuanghong-Huo-720x720-1.jpg\",\"datePublished\":\"2024-12-09T15:37:48+00:00\",\"dateModified\":\"2026-04-05T11:34:30+00:00\",\"inLanguage\":\"en-US\",\"potentialAction\":[{\"@type\":\"ReadAction\",\"target\":[\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/profiles\\\/shuanghong-huo\\\/\"]}]},{\"@type\":\"ImageObject\",\"inLanguage\":\"en-US\",\"@id\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/profiles\\\/shuanghong-huo\\\/#primaryimage\",\"url\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/wp-content\\\/uploads\\\/sites\\\/5\\\/2024\\\/12\\\/Shuanghong-Huo-720x720-1.jpg\",\"contentUrl\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/wp-content\\\/uploads\\\/sites\\\/5\\\/2024\\\/12\\\/Shuanghong-Huo-720x720-1.jpg\",\"width\":720,\"height\":720,\"caption\":\"Shuanghong Huo\"},{\"@type\":\"BreadcrumbList\",\"@id\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/wp-json\\\/wp\\\/v2\\\/cu_faculty\\\/95#breadcrumbs\",\"itemListElement\":[{\"@type\":\"ListItem\",\"position\":0,\"name\":\"ClarkU\",\"item\":\"https:\\\/\\\/www.clarku.edu\\\/\"},{\"@type\":\"ListItem\",\"position\":1,\"name\":\"Faculty\",\"item\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\"},{\"@type\":\"ListItem\",\"position\":2,\"name\":\"Profiles\",\"item\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/wp-json\"},{\"@type\":\"ListItem\",\"position\":3,\"name\":\"Profiles\",\"item\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/wp-json\\\/wp\"},{\"@type\":\"ListItem\",\"position\":4,\"name\":\"Profiles\",\"item\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/wp-json\\\/wp\\\/v2\"},{\"@type\":\"ListItem\",\"position\":5,\"name\":\"Profiles\",\"item\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/wp-json\\\/wp\\\/v2\\\/cu_faculty\"},{\"@type\":\"ListItem\",\"position\":6,\"name\":\"Profiles\",\"item\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/wp-json\\\/wp\\\/v2\\\/cu_faculty\\\/95\"}]},{\"@type\":\"WebSite\",\"@id\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/#website\",\"url\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/\",\"name\":\"Faculty\",\"description\":\"\",\"potentialAction\":[{\"@type\":\"SearchAction\",\"target\":{\"@type\":\"EntryPoint\",\"urlTemplate\":\"https:\\\/\\\/www.clarku.edu\\\/faculty\\\/?s={search_term_string}\"},\"query-input\":{\"@type\":\"PropertyValueSpecification\",\"valueRequired\":true,\"valueName\":\"search_term_string\"}}],\"inLanguage\":\"en-US\"}]}<\/script>\n<!-- \/ Yoast SEO Premium plugin. -->","yoast_head_json":{"title":"Shuanghong Huo | Faculty","robots":{"index":"index","follow":"follow","max-snippet":"max-snippet:-1","max-image-preview":"max-image-preview:large","max-video-preview":"max-video-preview:-1"},"canonical":"https:\/\/www.clarku.edu\/faculty\/profiles\/shuanghong-huo\/","og_locale":"en_US","og_type":"article","og_title":"Shuanghong Huo","og_description":"Sharon Huo graduated from Peking University in 1990, majoring in Applied Chemistry. 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