{"id":824,"date":"2024-12-18T10:25:55","date_gmt":"2024-12-18T15:25:55","guid":{"rendered":"https:\/\/www.golive.clarku.edu\/faculty\/profiles\/don-spratt\/"},"modified":"2026-04-05T17:07:58","modified_gmt":"2026-04-05T21:07:58","slug":"don-spratt","status":"publish","type":"cu_faculty","link":"https:\/\/www.clarku.edu\/faculty\/profiles\/don-spratt\/","title":{"rendered":"Don Spratt"},"content":{"rendered":"<p>Don Spratt is a Professor in the Gustaf H. Carlson School of Chemistry &amp; Biochemistry and the Director of STEM Summer Undergraduate Research Opportunities at Clark University. His NIH and MLSC funded research group focuses on the structural and mechanistic studies of the HECT E3 ubiquitin ligases and homeodomain transcription factors using biophysical approaches. Dr. Spratt was a 2021 Jack W. Lund Clark Community Achievement Awardee, a 2024 New England Biolabs Passion for Science Awardee in Scientific Mentorship and Advocacy, and a 2025 Clark University Faculty Urban Fellowship for his initiative to make STEM education and laboratory research experience real for hundreds of high school students across the Worcester region. He was a 2022 Hodgkins Junior Faculty Awardee for excellence in research, teaching, and service. He is an active member of the Protein Society. For Summer 2025, he worked as the Academic Director for the Summer Science Program International (ssp.org) at Purdue University where he engaged with 36 domestic and international high school students in hands-on biochemical research of enzymes, effective science communication, and soft skill development.\u00a0<\/p>\n<p>Prior to joining Clark University in 2015, he was a postdoctoral fellow and research associate in the Department of Biochemistry at the University of Western Ontario where he examined proteins involved in the ubiquitylation-signaling pathway. He was the recipient of postdoctoral fellowship awards from the Canadian Institutes of Health Research, the Natural Sciences and Engineering Research Council of Canada, and the Ontario Ministry of Research and Innovation. He received his Ph.D. in Chemistry from the University of Waterloo and his B.Sc. in Biochemistry from Mount Allison University.<\/p>\n<p>Courses Offered:<br \/>BCMB 271 &#8211; Foundations in Biochemistry (Lecture &amp; Lab)<br \/>BCMB 272 &#8211; Carbohydrate Metabolism<br \/>BCMB 275 &#8211; Protein Chemistry<br \/>BCMB 277 &#8211; Enzyme Reaction Mechanisms<br \/>CHEM 030 &#8211; Kitchen Chemistry (Lecture &amp; Lab)<br \/>CHEM 289 &#8211; LEEPing into a Science Career<span style=\"color:#000000;font-size:14.666666984558105px;font-style:normal;font-weight:normal;text-decoration:none\"><br \/><\/span><span style=\"color:#000000;font-size:14.666666984558105px;font-style:normal;font-weight:normal;text-decoration:none\"><\/span><\/p>\n","protected":false},"author":0,"featured_media":1977,"parent":0,"template":"","meta":{"cu_faculty_f180_userid":"C70230467","cu_faculty_first_name":"Don","cu_faculty_last_name":"Spratt","cu_faculty_employment_status":"Full Time","cu_faculty_rank":"Professor","cu_faculty_position":"Professor","cu_faculty_phone":"","cu_faculty_email":"DSpratt@clarku.edu","cu_faculty_location":"","cu_faculty_about":"<p>Don Spratt is a Professor in the Gustaf H. Carlson School of Chemistry &amp; Biochemistry and the Director of STEM Summer Undergraduate Research Opportunities at Clark University. His NIH and MLSC funded research group focuses on the structural and mechanistic studies of the HECT E3 ubiquitin ligases and homeodomain transcription factors using biophysical approaches. Dr. Spratt was a 2021 Jack W. Lund Clark Community Achievement Awardee, a 2024 New England Biolabs Passion for Science Awardee in Scientific Mentorship and Advocacy, and a 2025 Clark University Faculty Urban Fellowship for his initiative to make STEM education and laboratory research experience real for hundreds of high school students across the Worcester region. He was a 2022 Hodgkins Junior Faculty Awardee for excellence in research, teaching, and service. He is an active member of the Protein Society. For Summer 2025, he worked as the Academic Director for the Summer Science Program International (ssp.org) at Purdue University where he engaged with 36 domestic and international high school students in hands-on biochemical research of enzymes, effective science communication, and soft skill development.\u00a0<br><br>Prior to joining Clark University in 2015, he was a postdoctoral fellow and research associate in the Department of Biochemistry at the University of Western Ontario where he examined proteins involved in the ubiquitylation-signaling pathway. He was the recipient of postdoctoral fellowship awards from the Canadian Institutes of Health Research, the Natural Sciences and Engineering Research Council of Canada, and the Ontario Ministry of Research and Innovation. He received his Ph.D. in Chemistry from the University of Waterloo and his B.Sc. in Biochemistry from Mount Allison University.<br><br>Courses Offered:<br>BCMB 271 - Foundations in Biochemistry (Lecture &amp; Lab)<br>BCMB 272 - Carbohydrate Metabolism<br>BCMB 275 - Protein Chemistry<br>BCMB 277 - Enzyme Reaction Mechanisms<br>CHEM 030 - Kitchen Chemistry (Lecture &amp; Lab)<br>CHEM 289 - LEEPing into a Science Career<span style=\"color:#000000;font-size:14.666666984558105px;font-style:normal;font-weight:normal;text-decoration:none;\"><br><\/span><span style=\"color:#000000;font-size:14.666666984558105px;font-style:normal;font-weight:normal;text-decoration:none;\"><\/span><\/p>","cu_faculty_degrees":"<span>Ph.D. in Chemistry,<\/span> University of Waterloo, 2008\n<span>B.S. in Biochemistry,<\/span> Mount Allison University, 2003","cu_faculty_cv":"https:\/\/faculty180.interfolio.com\/public\/download.php?key=SDRwNCtxSUpsamxBQ213WS9ucHFuNnMwT0hzQU11b2RPQkJ2cWc3amxyUmNRdVVXTkF4MU1zT21qREtJZEdWZ1k0R2RXNmh1SG9laVFhK0V3R2hDZHpIN2xiRWlZbUplYXNUMlBBRzVtZW1HcUJTK05aU3FSQT09","cu_faculty_links":"{\"Professional Website URL\":\"https:\\\/\\\/wordpress.clarku.edu\\\/dspratt\\\/\",\"ORCID ID\":\"HTTPS:\\\/\\\/ORCID.ORG\\\/0000-0002-0699-155X\",\"Google Scholar\":\"https:\\\/\\\/scholar.google.ca\\\/citations?user=yK4ce2EAAAAJ&amp;hl=en\",\"Research Gate\":\"HTTP:\\\/\\\/WWW.RESEARCHGATE.NET\\\/PROFILE\\\/DONALD_SPRATT\"}","cu_faculty_scholarly_interests":"Enzymes, Ubiquitin, HECT E3 Ubiquitin Ligases, Homeodomain Transcription Factors, NMR Spectroscopy, Protein-Protein\/DNA Interactions, STEM Outreach, Career Development","cu_faculty_scholarly_works":"[{\"activityid\":13484,\"fields\":{\"Type\":\"Articles in Refereed Journals\",\"Title\":\"&lt;p&gt;Experimental approaches to investigate biophysical interactions between homeodomain transcription factors and DNA&lt;\\\/p&gt;\",\"Journal Title\":\"Biochimica et biophysica acta. Gene regulatory mechanisms\",\"Series Title\":\"\",\"Month \\\/ Season\":\"\",\"Year\":2025,\"Publisher\":\"\",\"Publisher City and State\":\"\",\"Publisher Country\":\"\",\"Volume\":\"1868\",\"Issue Number \\\/ Edition\":\"1\",\"Page Number(s) or Number of Pages\":\"195074\",\"ISSN\":\"\",\"DOI\":\"\",\"CoAuthor\":null,\"URL\":\"https:\\\/\\\/www.sciencedirect.com\\\/science\\\/article\\\/pii\\\/S1874939924000701\",\"Description\":\"&lt;p&gt;Homeodomain transcription factors (TFs) bind to specific DNA sequences to regulate the expression of target genes. Structural work has provided insight into molecular identities and aided in unraveling structural features of these TFs. However, the detailed affinity and specificity by which these TFs bind to DNA sequences is still largely unknown. Qualitative methods, such as DNA footprinting, Electrophoretic Mobility Shift Assays (EMSAs), Systematic Evolution of Ligands by Exponential Enrichment (SELEX), Bacterial One Hybrid (B1H) systems, Surface Plasmon Resonance (SPR), and Protein Binding Microarrays (PBMs) have been widely used to investigate the biochemical characteristics of TF-DNA binding events. In addition to these qualitative methods, bioinformatic approaches have also assisted in TF binding site discovery. Here we discuss the advantages and limitations of these different approaches, as well as the benefits of utilizing more quantitative approaches, such as Mechanically Induced Trapping of Molecular Interactions (MITOMI), Microscale Thermophoresis (MST) and Isothermal Titration Calorimetry (ITC), in determining the biophysical basis of binding specificity of TF-DNA complexes and improving upon existing computational approaches aimed at affinity predictions.&lt;\\\/p&gt;\",\"Include description in output citation\":0,\"Origin\":\"PubMed\"},\"facultyid\":\"C70230467\",\"status\":[{\"id\":13484,\"status\":\"Completed\\\/Published\",\"term\":\"Spring\",\"year\":2025,\"termid\":\"2024\\\/03\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[{\"attachmentid\":12030,\"mimetype\":\"application\\\/pdf\",\"filename\":\"Experimental approaches to investigate biophysical interactions b.pdf\",\"filesize\":10005339,\"downloadurl\":\"https:\\\/\\\/faculty180.interfolio.com\\\/public\\\/download.php?key=SDRwNCtxSUpsamxBQ213WS9ucHFuNnMwT0hzQU11b2RPQkJ2cWc3amxyUmNRdVVXTkF4MU1zT21qREtJZEdWZ2NlN3RDdkJidis1cHVycUhPamh1WmR6UW5yUDhKZUxUazhjZERzNWNnMHJEeXVic0VmVUdzSmo1aTlXaitjT2JoVTlydWk2UGF6NHZTbWZlc2xWb2RJS3B5ZXNONVVmRkE5bXNnRE8zSExOWHpiK0Nra0FOdXc9PQ%3D%3D\"}],\"coauthors_list\":[\"Fadwa Mekkaoui\",\"Robert A Drewell\",\"Jacqueline M Dresch\",\"Donald E Spratt\"],\"sort_date\":\"2025-1-01\"},{\"activityid\":13485,\"fields\":{\"Type\":\"Articles in Refereed Journals\",\"Title\":\"&lt;p&gt;The disordered negatively charged C-terminus of the large HECT E3 ubiquitin ligase HERC2 provides structural and thermal stability to the HECT C-lobe&lt;\\\/p&gt;\",\"Journal Title\":\"Protein science : a publication of the Protein Society\",\"Series Title\":\"\",\"Month \\\/ Season\":\"\",\"Year\":2024,\"Publisher\":\"\",\"Publisher City and State\":\"\",\"Publisher Country\":\"\",\"Volume\":\"33\",\"Issue Number \\\/ Edition\":\"12\",\"Page Number(s) or Number of Pages\":\"e5229\",\"ISSN\":\"\",\"DOI\":\"\",\"CoAuthor\":null,\"URL\":\"https:\\\/\\\/onlinelibrary.wiley.com\\\/doi\\\/10.1002\\\/pro.5229\",\"Description\":\"&lt;p&gt;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.&lt;\\\/p&gt;\",\"Include description in output citation\":0,\"Origin\":\"PubMed\"},\"facultyid\":\"C70230467\",\"status\":[{\"id\":13485,\"status\":\"Completed\\\/Published\",\"term\":\"Fall\",\"year\":2024,\"termid\":\"2024\\\/01\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[{\"attachmentid\":12029,\"mimetype\":\"application\\\/pdf\",\"filename\":\"Protein Science - 2024 - Waters - The disordered negatively charged C%E2%80%90terminus of the large HECT E3 ubiquitin ligase HERC2.pdf\",\"filesize\":4228376,\"downloadurl\":\"https:\\\/\\\/faculty180.interfolio.com\\\/public\\\/download.php?key=SDRwNCtxSUpsamxBQ213WS9ucHFuNnMwT0hzQU11b2RPQkJ2cWc3amxyUmNRdVVXTkF4MU1zT21qREtJZEdWZ2NlN3RDdkJidis1L1JuYjVtVmZsUTBsVU8rYUM1VHduQUdYc1FrL2h4cno5U1R3UVNCVHN6Y2VEQlRYZkRBRGU5N0xPbHBwSjRuWmFqYStmVkRNazl6cDdSZHRnMkRXbHc2TnFKa25jOWlwVHI1UHlZMS9GVng2MGxHTFRwa3hKY3JMdFdCWWJiSmtpZFp3VHBxaGdTbW9rblBNTUx0RE5TQXJYT3QxT1RKd0lVODNEVy91NnlkMjlLUVlkakJVeVplT0dDbUtDZWc4cUliK0F3cjlUdEE9PQ%3D%3D\"}],\"coauthors_list\":[\"Kelly L Waters\",\"Kayla J Rich\",\"Noah D Schwaegerle\",\"Tianyi Yang\",\"Shuanghong Huo\",\"Donald E Spratt\"],\"sort_date\":\"2024-9-01\"},{\"activityid\":10435,\"fields\":{\"Type\":\"Presentations\",\"Title of Presentation\":\"&lt;span style=&quot;font-size:10pt;&quot;&gt;Structural characterization of the ankyrin-repeat containing oncoprotein gankyrin in the presence of small molecules&lt;\\\/span&gt;\",\"Conference \\\/ Meeting Name\":\"The Tumor Ecosystem: Cellular Interactions and Therapeutic Opportunities\",\"Location of Conference \\\/ Meeting\":\"Bergamo, Italy\",\"Month \\\/ Season\":\"March\",\"Year\":2024,\"Sponsoring Organization\":\"European Association for Cancer Research\",\"CoAuthor\":null,\"URL\":\"\",\"Description\":\"\",\"Include description in output citation\":0,\"Origin\":\"Manual\"},\"facultyid\":\"C70230467\",\"status\":[{\"id\":10435,\"status\":\"Completed\\\/Published\",\"term\":\"Spring\",\"year\":2024,\"termid\":\"2023\\\/03\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[],\"coauthors_list\":[\"Maryam Riyazi\",\"Taylor M. Laflamme\",\"Dipti Kanabar\",\"T Chavan\",\"Aaron Muth\",\"Don E. Spratt\"],\"sort_date\":\"2024-3-01\"},{\"activityid\":10432,\"fields\":{\"Type\":\"Presentations\",\"Title of Presentation\":\"&lt;span style=&quot;font-size:10pt;&quot;&gt;Development of a kinetic FRET-based assay for the study of HECT E3 ligase inhibition by small molecules&lt;\\\/span&gt;\",\"Conference \\\/ Meeting Name\":\"49th Lorne Conference on Protein Structure and Function\",\"Location of Conference \\\/ Meeting\":\"Lorne, Australia\",\"Month \\\/ Season\":\"February\",\"Year\":2024,\"Sponsoring Organization\":\"\",\"CoAuthor\":null,\"URL\":\"\",\"Description\":\"\",\"Include description in output citation\":0,\"Origin\":\"Manual\"},\"facultyid\":\"C70230467\",\"status\":[{\"id\":10432,\"status\":\"Completed\\\/Published\",\"term\":\"Spring\",\"year\":2024,\"termid\":\"2023\\\/03\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[],\"coauthors_list\":[\"Amanda R. Brown\",\"Don E. Spratt\"],\"sort_date\":\"2024-2-01\"},{\"activityid\":10433,\"fields\":{\"Type\":\"Presentations\",\"Title of Presentation\":\"&lt;span style=&quot;font-size:10pt;color:#000000;&quot;&gt;Structural impacts of small molecule drugs targeting the ankyrin repeat oncoprotein gankyrin&lt;\\\/span&gt;\",\"Conference \\\/ Meeting Name\":\"49th Lorne Conference on Protein Structure and Function\",\"Location of Conference \\\/ Meeting\":\"Lorne, Australia\",\"Month \\\/ Season\":\"February\",\"Year\":2024,\"Sponsoring Organization\":\"\",\"CoAuthor\":null,\"URL\":\"\",\"Description\":\"\",\"Include description in output citation\":0,\"Origin\":\"Manual\"},\"facultyid\":\"C70230467\",\"status\":[{\"id\":10433,\"status\":\"Completed\\\/Published\",\"term\":\"Spring\",\"year\":2024,\"termid\":\"2023\\\/03\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[],\"coauthors_list\":[\"Taylor M. Laflamme\",\"Emma I. Kane\",\"Maryam Riyazi\",\"Dipti Kanabar\",\"T Chavan\",\"Aaron Muth\",\"Don E. Spratt\"],\"sort_date\":\"2024-2-01\"},{\"activityid\":10434,\"fields\":{\"Type\":\"Presentations\",\"Title of Presentation\":\"&lt;span style=&quot;font-size:10pt;color:#000000;&quot;&gt;Apo-calmodulin binds to the HECT E3 ubiquitin ligase UBE3C via its N-terminal IQ motif&lt;\\\/span&gt;\",\"Conference \\\/ Meeting Name\":\"49th Lorne Conference on Protein Structure and Function\",\"Location of Conference \\\/ Meeting\":\"Lorne, Australia\",\"Month \\\/ Season\":\"February\",\"Year\":2024,\"Sponsoring Organization\":\"\",\"CoAuthor\":null,\"URL\":\"\",\"Description\":\"\",\"Include description in output citation\":0,\"Origin\":\"Manual\"},\"facultyid\":\"C70230467\",\"status\":[{\"id\":10434,\"status\":\"Completed\\\/Published\",\"term\":\"Spring\",\"year\":2024,\"termid\":\"2023\\\/03\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[],\"coauthors_list\":[\"Emily G. Schaffter\",\"Megan R. Hill\",\"Don E. Spratt\"],\"sort_date\":\"2024-2-01\"},{\"activityid\":10414,\"fields\":{\"Type\":\"Articles in Refereed Journals\",\"Title\":\"&lt;p&gt;Synthesis and evaluation of 2,5-substituted pyrimidines as small-molecule gankyrin binders&lt;\\\/p&gt;\",\"Journal Title\":\"Future medicinal chemistry\",\"Series Title\":\"\",\"Month \\\/ Season\":\"\",\"Year\":2024,\"Publisher\":\"\",\"Publisher City and State\":\"\",\"Publisher Country\":\"\",\"Volume\":\"16\",\"Issue Number \\\/ Edition\":\"3\",\"Page Number(s) or Number of Pages\":\"239-251\",\"ISSN\":\"\",\"DOI\":\"10.4155\\\/fmc-2023-0124\",\"CoAuthor\":null,\"URL\":\"https:\\\/\\\/www.tandfonline.com\\\/doi\\\/10.4155\\\/fmc-2023-0124\",\"Description\":\"&lt;p&gt;&lt;b&gt;Background:&lt;\\\/b&gt;&lt;span&gt; Gankyrin is an ankyrin-repeat protein that promotes cell proliferation, tumor development and cancer progression when overexpressed. &lt;\\\/span&gt;&lt;b&gt;Aim:&lt;\\\/b&gt;&lt;span&gt; To design and synthesize a novel series of gankyrin-binding small molecules predicated on a 2,5-pyrimidine scaffold. &lt;\\\/span&gt;&lt;b&gt;Materials &amp; methods:&lt;\\\/b&gt;&lt;span&gt; The synthesized compounds were evaluated for their antiproliferative activity, ability to bind gankyrin and effects on cell cycle progression and the proteasomal degradation pathway. &lt;\\\/span&gt;&lt;b&gt;Results:&lt;\\\/b&gt;&lt;span&gt; Compounds &lt;\\\/span&gt;&lt;b&gt;188&lt;\\\/b&gt;&lt;span&gt; and &lt;\\\/span&gt;&lt;b&gt;193&lt;\\\/b&gt;&lt;span&gt; demonstrated the most potent antiproliferative activity against MCF7 and A549 cells, respectively. Both compounds also demonstrated the ability to effectively bind gankyrin, disrupt proteasomal degradation and inhibit cell cycle progression. &lt;\\\/span&gt;&lt;b&gt;Conclusion:&lt;\\\/b&gt;&lt;span&gt; The 2,5-pyrimidine scaffold exhibits a novel and promising strategy for binding gankyrin and inhibiting cancer cell proliferation.&lt;\\\/span&gt;&lt;\\\/p&gt;\",\"Include description in output citation\":0,\"Origin\":\"PubMed\"},\"facultyid\":\"C70230467\",\"status\":[{\"id\":10414,\"status\":\"Completed\\\/Published\",\"term\":\"Spring\",\"year\":2024,\"termid\":\"2023\\\/03\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[{\"attachmentid\":12031,\"mimetype\":\"application\\\/pdf\",\"filename\":\"Synthesis and Evaluation of 2,5-Substituted Pyrimidines as Small-Molecule Gankyrin Binders: Future M.pdf\",\"filesize\":244359,\"downloadurl\":\"https:\\\/\\\/faculty180.interfolio.com\\\/public\\\/download.php?key=SDRwNCtxSUpsamxBQ213WS9ucHFuNnMwT0hzQU11b2RPQkJ2cWc3amxyUmNRdVVXTkF4MU1zT21qREtJZEdWZ2NlN3RDdkJidis3SHlrRXY1QWRocnFETjhYZ2x5OUw2NTVtSE9BMlY3Qk1kQjZEWlFjanhFSnp5TG9kQVlJK2lpSjdMNlo2VStRc1pkYXRWMGJCS2hDdm0yRmpSOUtadXUyODRTSFdVSkw5MjRSalFwVzYraFVid08wTEpFWUFtVFR5M0wzS2JKbkVLeFR3ZmZ2WEdERWt4bmROL3Yzc21LaUcvZ01LL1U3UT0%3D\"}],\"coauthors_list\":[\"Dipti Kanabar\",\"Emma I Kane\",\"Tejashri Chavan\",\"Taylor M Laflamme\",\"Ethan Suarez\",\"Mimansa Goyal\",\"Vivek Gupta\",\"Donald E Spratt\",\"Aaron Muth\"],\"sort_date\":\"2024-1-01\"},{\"activityid\":10416,\"fields\":{\"Type\":\"Articles in Refereed Journals\",\"Title\":\"New Discoveries on Protein Recruitment and Regulation during the Early Stages of the DNA Damage Response Pathways\",\"Journal Title\":\"International journal of molecular sciences\",\"Series Title\":\"\",\"Month \\\/ Season\":\"\",\"Year\":2024,\"Publisher\":\"\",\"Publisher City and State\":\"\",\"Publisher Country\":\"\",\"Volume\":\"25\",\"Issue Number \\\/ Edition\":\"3\",\"Page Number(s) or Number of Pages\":\"\",\"ISSN\":\"\",\"DOI\":\"10.3390\\\/ijms25031676\",\"CoAuthor\":null,\"URL\":\"https:\\\/\\\/www.mdpi.com\\\/1422-0067\\\/25\\\/3\\\/1676\",\"Description\":\"\",\"Include description in output citation\":0,\"Origin\":\"PubMed\"},\"facultyid\":\"C70230467\",\"status\":[{\"id\":10416,\"status\":\"Completed\\\/Published\",\"term\":\"Intersession\",\"year\":2024,\"termid\":\"2023\\\/02\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[{\"attachmentid\":8775,\"mimetype\":\"application\\\/pdf\",\"filename\":\"ijms-25-01676.pdf\",\"filesize\":8083720,\"downloadurl\":\"https:\\\/\\\/faculty180.interfolio.com\\\/public\\\/download.php?key=SDRwNCtxSUpsamxBQ213WS9ucHFuNnMwT0hzQU11b2RPQkJ2cWc3amxyUmNRdVVXTkF4MU1zT21qREtJZEdWZ2svSVMxNmxQSE5HeExveStkWlZycTRsb2ovOXBKR3JqdHAzQzVwVnc3UTE4c1UzNWVONWJhZz09\"}],\"coauthors_list\":[\"Kelly L Waters\",\"Donald E Spratt\"],\"sort_date\":\"2024-1-01\"},{\"activityid\":13486,\"fields\":{\"Type\":\"Articles in Refereed Journals\",\"Title\":\"&lt;p&gt;Structural modification of the propyl linker of cjoc42 in combination with sulfonate ester and triazole replacements for enhanced gankyrin binding and anti-proliferative activity&lt;\\\/p&gt;\",\"Journal Title\":\"Bioorganic &amp; medicinal chemistry\",\"Series Title\":\"\",\"Month \\\/ Season\":\"\",\"Year\":2024,\"Publisher\":\"\",\"Publisher City and State\":\"\",\"Publisher Country\":\"\",\"Volume\":\"110\",\"Issue Number \\\/ Edition\":\"\",\"Page Number(s) or Number of Pages\":\"117836\",\"ISSN\":\"\",\"DOI\":\"\",\"CoAuthor\":null,\"URL\":\"https:\\\/\\\/www.sciencedirect.com\\\/science\\\/article\\\/abs\\\/pii\\\/S0968089624002505\",\"Description\":\"&lt;p&gt;Liver cancer is a complex disease that involves various oncoproteins and the inactivation of tumor suppressor proteins (TSPs). Gankyrin is one such oncoprotein, first identified in human hepatocellular carcinoma, that is known to inactivate multiple TSPs, leading to proliferation and metastasis of tumor cells. Despite this, there has been limited development of small molecule gankyrin binders for the treatment of liver cancer. In this study, we are reporting the structure-based design of gankyrin-binding small molecules which inhibit the proliferation of HuH6 and HepG2 cells while also increasing the levels of certain TSPs, such as Rb and p53. Interestingly the first molecule to exhibit inhibition by 3D structure stabilization is seen. These results suggest a possible mechanism for small-molecule inhibition of gankyrin and demonstrate that gankyrin is a viable therapeutic target for the treatment of liver cancer.&lt;\\\/p&gt;\",\"Include description in output citation\":0,\"Origin\":\"PubMed\"},\"facultyid\":\"C70230467\",\"status\":[{\"id\":13486,\"status\":\"Completed\\\/Published\",\"term\":\"Summer\",\"year\":2024,\"termid\":\"2023\\\/05\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[{\"attachmentid\":12028,\"mimetype\":\"application\\\/pdf\",\"filename\":\"Structural modification of the propyl linker of cjoc42 in combination with sulfonate ester and triaz.pdf\",\"filesize\":356884,\"downloadurl\":\"https:\\\/\\\/faculty180.interfolio.com\\\/public\\\/download.php?key=SDRwNCtxSUpsamxBQ213WS9ucHFuNnMwT0hzQU11b2RPQkJ2cWc3amxyUmNRdVVXTkF4MU1zT21qREtJZEdWZ2NlN3RDdkJidis1MXdWdnVjcnRoamxCcXVaMTNoaEwvaVJ2M1dTaDc5dEZGZkhQUS8zOXJSRGU4cDduMVNUdFlaczhPcUkxdkQ0Y0xscGVxUU9nOXpiemVWM0dqZzN6bEpuYUZVNDZGcDRVdC9RRXFsa0RyOUR6N0JUcEpSa0Vnangwbm5LcjZmaEJDYWsvRnRqenBKSDE3d0NNVENyU09mTEZOK1hqZVcybz0%3D\"}],\"coauthors_list\":[\"Tejashri Chavan\",\"Dipti Kanabar\",\"Kinjal Patel\",\"Taylor M Laflamme\",\"Maryam Riyazi\",\"Donald E Spratt\",\"Aaron Muth\"],\"sort_date\":\"2024-1-01\"},{\"activityid\":10431,\"fields\":{\"Type\":\"Other Media (social media, blogs, podcasts, etc)\",\"Title\":\"ClarkNOW\",\"Episode Title\":\"From the periodic table to the kitchen table\",\"Date Published\":\"2023-12-14\",\"Year\":2023,\"Platform\":\"Website &amp; Social Media\",\"CoAuthor\":null,\"URL\":\"https:\\\/\\\/clarknow.clarku.edu\\\/2023\\\/12\\\/14\\\/from-the-periodic-table-to-the-kitchen-table\\\/\",\"Description\":\"\",\"Include description in output citation\":0,\"Origin\":\"Manual\"},\"facultyid\":\"C70230467\",\"status\":[{\"id\":10431,\"status\":\"Completed\\\/Published\",\"term\":\"Fall\",\"year\":2023,\"termid\":\"2023\\\/01\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[],\"coauthors_list\":[\"Don E. 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press\",\"CoAuthor\":null,\"URL\":\"https:\\\/\\\/diverseeducation.com\\\/article\\\/188408\\\/\",\"Description\":\"Be nice!\\n\\nWe\\u2019ve all heard about six degrees of separation \\u2013 the idea that everyone on the planet are six or fewer connections away from one another (i.e. \\u201cfriend of a friend\\u201d).  In the science world, it\\u2019s more like three degrees of separation.  The science community is small, so to have a successful and fulfilling career in science it is important to always be kind and collaborative.  Scientists talk with each other, especially when it comes to potentially hiring someone for their research group or company.  Hiring committees are increasingly more cautious when hiring and perform their due diligence by having online background checks and\\\/or speaking directly with references over the phone or by Skype for job candidates.  The proverb, \\u201cPeople may not remember exactly what you did or what you said, but they will always remember how you made them feel\\u201d is very applicable in science.  First impressions matter and you want to make sure you leave a positive impression with everyone you meet during an interview.  Having polite email and phone correspondence with your interviewers before, during, and after an interview is an also important yet commonly overlooked aspect of securing a job in STEM.  Companies want to hire talented people that will strengthen the atmosphere and culture of their workplace and have the potential to grow into a contributing member of their team.  So please \\u2013 be polite, be punctual, and above all, be nice.\\n\\nDr. Donald E. Spratt\\n\\nNetwork, Network, Network!\\n\\nMaking meaningful connections is vital to becoming successful in science.  Serendipity is an amazing phenomenon where chance encounters can create lucky opportunities and open doors to new careers for you that you may have never considered before. Expanding your network can also help you identify potential mentors that can give you invaluable guidance on how to navigate your next steps in your career.  For some young scientists that are introverts, this can be a daunting or downright terrifying experience. Don\\u2019t be shy \\u2013 many senior scientists are ready, willing and eager to support the next generation of scientists navigate the job market.  A great venue to grow your network is at conferences \\u2013 each person that comes to your talk or by your poster to learn about your research could potentially become a new network connection. There are also career workshops held around the country that could be a good platform for you to learn more about STEM career options.  Many universities and colleges have started to build their own LinkedIn-like platforms to connect students with potential internships or jobs, with many alumni joining these social networks to actively help and\\\/or recruit from their alma mater.  Informational interviews are another great way to build your network where you can gather firsthand information from an expert about the realities of working within a particular field and are an excellent way to learn more about a potential career or company environment before you apply for a job.  Get out there and make a new connection or friend in the science community!\\n\\nBe tenacious and strive for excellence!\\n\\nMany science students work long hours in the lab thinking that if they work hard enough they will get that elusive result to complete their thesis or to publish a paper in an illustrious journal.  For some this approach will lead to success; for others, the upsetting reality is that their project might not work out and they will struggle with feelings of disappointment.  This can sometimes make young scientists question why they are in the field at all.  Surround yourself with smart people in a positive work environment that will support your career growth and give you the mentorship you need at the right time.  Tenacity, patience, and stick-to-itiveness are the hallmarks of a successful scientist.  \\u201cDust yourself off and get back in the ring\\u201d is an excellent phrase to keep motivated and approach your career in STEM \\u2013 never give up!\\n\\nDon\\u2019t be afraid of take on a new challenge!\\n\\nTechniques learned in classroom or the lab are often translatable to other science fields.  Just because you worked in a specific area of research doesn\\u2019t mean you have to work in that area for your entire career.  Many successful scientists adapt and take on challenging projects that peak their interest.  I would argue that the true measure of the mettle of a scientist is not specific techniques or lab skills they have mastered, but the actual approach they take to answer the scientific question they want to answer that matters.  Most interviewers are not particularly interested in hearing a long drawn out discussion on your research thesis you completed last month or a few years ago \\u2013 they want the short, snappy two-minute synopsis.  They are more interested in hearing about how you approached a challenging problem and if you were able to overcome an obstacle leading to success.\\n\\nIt is also important for all scientists to become effective communicators to share our knowledge and love of the natural world with the general public.  Scientists have a role to play in helping to improve scientific literacy for the masses \\u2013 whether it be at work, in your community, or at a party \\u2013 as well as inspiring the next generation of students to pursue careers in STEM.  While this can be challenging, it is vital that young scientists joining the workforce step up to help shape the narrative for how science is perceived in this day of misinformation and sensational headlines \\u2013 let\\u2019s all work together to cut through the noise.\\n\\nAlways be passionate about science and never stop learning!\\n\\nMany strong resumes these days list the techniques that people have mastered, which is a good thing.  But what separates the good candidates from the amazing candidates during their interviews is their undeniable and overflowing love for science.  All employers are looking for people that are excited and passionate about research and want to build a team of smart and welcoming thinkers.  I teach many students that work in my research lab or have taken my classes that \\u201cscience is not a race, it\\u2019s a journey!\\u201d  It is a life-long and noble pursuit.  Always be curious and try to carve out time in your schedule to learn about new developments and advances in your field.  Go to a symposium, listen to podcasts, read books and magazines \\u2013 expand your mind and scientific interests.  Learning doesn\\u2019t stop when you close your last text book or write your final exam \\u2013 science is always evolving and it is important that you stay engaged and grow with the science community.\\n\\nDr. Donald E. Spratt is an assistant professor of chemistry and biochemistry at Clark University. \",\"Include description in output citation\":0,\"Origin\":\"Manual\"},\"facultyid\":\"C70230467\",\"status\":[{\"id\":3790,\"status\":\"Completed\\\/Published\",\"term\":\"Summer\",\"year\":2020,\"termid\":\"2019\\\/05\",\"listingorder\":6,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[],\"coauthors_list\":[\"Donald E. 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We will elucidate the underlying biochemical and structural basis for the anti-viral role of HERC5 that can aid in the development of future viral treatments and improve human health. &lt;\\\/span&gt;&lt;\\\/p&gt;\",\"Number of Periods\":1,\"URL\":\"\"},\"facultyid\":\"C70230467\",\"funding\":{\"6906\":{\"id\":6906,\"grantid\":1755,\"fundedamount\":\"450900\",\"yearfunded\":1,\"fundedtype\":\"Total\",\"currencytype\":\"USD\",\"startdate\":\"2022-05-01\",\"enddate\":\"2023-05-01\"},\"6907\":{\"id\":6907,\"grantid\":1755,\"fundedamount\":\"300000\",\"yearfunded\":1,\"fundedtype\":\"Direct\",\"currencytype\":\"USD\",\"startdate\":\"2022-05-01\",\"enddate\":\"2023-05-01\"}},\"coauthors\":{\"6373\":{\"authorid\":6373,\"grantid\":1755,\"firstname\":\"Donald\",\"middleinitial\":\"E.\",\"lastname\":\"Spratt\",\"authortype\":\"PI\",\"percenteffort\":null,\"sameschoolflag\":1,\"facultyid\":\"C70230467\",\"primaryunitid\":9}},\"status\":[{\"grantid\":1755,\"status\":\"Funded - In Progress\",\"statuslabel\":\"Funded - In Progress\",\"term\":\"Spring\",\"year\":2022,\"termid\":\"2021\\\/03\",\"listingorder\":3,\"completionorder\":5}],\"userid\":\"C70230467\",\"attachments\":[],\"sort_date\":\"2025-04-30\"},{\"activityid\":4028,\"fields\":{\"Title\":\"Clark University Biochemistry Outreach in Worcester MA: Protein Purification and Science Careers\",\"Sponsor\":\"The Protein Society\",\"Grant ID \\\/ Contract ID\":\"\",\"Award Date\":\"2023-09-11\",\"Start Date\":\"2023-09-11\",\"End Date\":\"2024-09-11\",\"Period Length\":1,\"Period Unit\":\"Year\",\"Indirect Funding\":0,\"Indirect Cost Rate\":null,\"Total Funding\":\"500\",\"Total Direct Funding\":null,\"Currency Type\":\"USD\",\"Description\":\"\",\"Abstract\":\"\",\"Number of Periods\":1,\"URL\":\"\"},\"facultyid\":\"C70230467\",\"funding\":{\"6919\":{\"id\":6919,\"grantid\":4028,\"fundedamount\":\"500\",\"yearfunded\":1,\"fundedtype\":\"Total\",\"currencytype\":\"USD\",\"startdate\":\"2023-09-11\",\"enddate\":\"2024-09-11\"}},\"coauthors\":{\"6385\":{\"authorid\":6385,\"grantid\":4028,\"firstname\":\"Don\",\"middleinitial\":\"E.\",\"lastname\":\"Spratt\",\"authortype\":\"PI\",\"percenteffort\":null,\"sameschoolflag\":1,\"facultyid\":\"C70230467\",\"primaryunitid\":9}},\"status\":[{\"grantid\":4028,\"status\":\"Funded - In Progress\",\"statuslabel\":\"Funded - In Progress\",\"term\":\"Fall\",\"year\":2023,\"termid\":\"2023\\\/01\",\"listingorder\":3,\"completionorder\":5}],\"userid\":\"C70230467\",\"attachments\":[],\"sort_date\":\"2024-09-11\"},{\"activityid\":4029,\"fields\":{\"Title\":\"Administrative Supplements for Equipment Purchases for Select NIGMS-Funded Awards\",\"Sponsor\":\"National Institute of General Medical Sciences\",\"Grant ID \\\/ Contract ID\":\"\",\"Award Date\":\"2023-07-10\",\"Start Date\":\"2023-07-10\",\"End Date\":\"2024-07-10\",\"Period Length\":1,\"Period Unit\":\"Year\",\"Indirect Funding\":0,\"Indirect Cost Rate\":null,\"Total Funding\":\"98045\",\"Total Direct Funding\":null,\"Currency Type\":\"USD\",\"Description\":\"\",\"Abstract\":\"\",\"Number of Periods\":1,\"URL\":\"\"},\"facultyid\":\"C70230467\",\"funding\":{\"6924\":{\"id\":6924,\"grantid\":4029,\"fundedamount\":\"98045\",\"yearfunded\":1,\"fundedtype\":\"Total\",\"currencytype\":\"USD\",\"startdate\":\"2023-07-10\",\"enddate\":\"2024-07-10\"}},\"coauthors\":{\"6390\":{\"authorid\":6390,\"grantid\":4029,\"firstname\":\"Don\",\"middleinitial\":\"E.\",\"lastname\":\"Spratt\",\"authortype\":\"PI\",\"percenteffort\":null,\"sameschoolflag\":1,\"facultyid\":\"C70230467\",\"primaryunitid\":9}},\"status\":[{\"grantid\":4029,\"status\":\"Completed\",\"statuslabel\":\"Completed\",\"term\":\"Summer\",\"year\":2023,\"termid\":\"2022\\\/05\",\"listingorder\":4,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[],\"sort_date\":\"2024-07-10\"},{\"activityid\":1756,\"fields\":{\"Title\":\"Using Computational Artificial Intelligence for Small Molecule Discovery to Drug the HECT E3 Ubiquitin Ligases\",\"Sponsor\":\"Atomwise, Inc.\",\"Grant ID \\\/ Contract ID\":\"AIMS Awards Program\",\"Award Date\":\"2021-10-03\",\"Start Date\":\"2021-12-01\",\"End Date\":\"2023-03-31\",\"Period Length\":1,\"Period Unit\":\"Year\",\"Indirect Funding\":0,\"Indirect Cost Rate\":null,\"Total Funding\":\"0\",\"Total Direct Funding\":null,\"Currency Type\":\"USD\",\"Description\":\"\",\"Abstract\":\"&lt;p&gt;As there are no available crystal structures of HECW2, a homology model was built with Swiss Model based on PDB ID 3JVZ (a NEDD4 family protein) as a template. The NEDD4 template is the appropriate model to use for the analysis of HECW2 as the two proteins have reasonable sequence identity, indicating that they may be very similar in structure. Since NEDD4 has been well studied and structurally characterized, this structure can be used to predict the less established structure of HECW2 to probe the E2 binding pocket. The indicated pocket was chosen as there is a druggable pocket (288.9 \\u00c53 in volume with a hydrophobicity of 0.51 and a buriedness of 0.78), and contains the site of a known missense mutation (F1327) linked to disease. 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Date\":\"2020-01-01\",\"End Date\":\"2020-12-31\",\"Period Length\":1,\"Period Unit\":\"Year\",\"Indirect Funding\":0,\"Indirect Cost Rate\":null,\"Total Funding\":\"2000\",\"Total Direct Funding\":null,\"Currency Type\":\"USD\",\"Description\":\"\",\"Abstract\":\"&lt;p&gt;This professional development internal grant program from the Dean of the Faculty is intended to train faculty on how to become ambassadors for the Clark University that can effectively communicate to the general population about their ongoing research projects.\\u00a0 This program involves regular meetings with other faculty from different disciplines across campus to discuss approaches to reach a general audience in effective ways.&lt;\\\/p&gt;\",\"Number of Periods\":1,\"URL\":\"\"},\"facultyid\":\"C70230467\",\"funding\":{\"2933\":{\"id\":2933,\"grantid\":222,\"fundedamount\":\"2000\",\"yearfunded\":1,\"fundedtype\":\"Total\",\"currencytype\":\"USD\",\"startdate\":\"2020-01-01\",\"enddate\":\"2021-01-01\"}},\"coauthors\":{\"2541\":{\"authorid\":2541,\"grantid\":222,\"firstname\":\"Donald\",\"middleinitial\":\"E.\",\"lastname\":\"Spratt\",\"authortype\":\"PI\",\"percenteffort\":null,\"sameschoolflag\":1,\"facultyid\":\"C70230467\",\"primaryunitid\":9}},\"status\":[{\"grantid\":222,\"status\":\"Completed\",\"statuslabel\":\"Completed\",\"term\":\"Spring\",\"year\":2020,\"termid\":\"2019\\\/03\",\"listingorder\":4,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[],\"sort_date\":\"2020-12-31\"},{\"activityid\":199,\"fields\":{\"Title\":\"Structure and Mechanism of HECT E3 Ubiquitin Ligases\",\"Sponsor\":\"National Institute of General Medical Sciences (NIGMS)\",\"Grant ID \\\/ Contract ID\":\"R15GM126432\",\"Award 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Periods\":1,\"URL\":\"\"},\"facultyid\":\"C70230467\",\"funding\":{\"2924\":{\"id\":2924,\"grantid\":199,\"fundedamount\":\"450900\",\"yearfunded\":1,\"fundedtype\":\"Total\",\"currencytype\":\"USD\",\"startdate\":\"2017-09-20\",\"enddate\":\"2018-09-20\"},\"2925\":{\"id\":2925,\"grantid\":199,\"fundedamount\":\"300000\",\"yearfunded\":1,\"fundedtype\":\"Direct\",\"currencytype\":\"USD\",\"startdate\":\"2017-09-20\",\"enddate\":\"2018-09-20\"}},\"coauthors\":{\"2536\":{\"authorid\":2536,\"grantid\":199,\"firstname\":\"Donald\",\"middleinitial\":\"E.\",\"lastname\":\"Spratt\",\"authortype\":\"PI\",\"percenteffort\":null,\"sameschoolflag\":1,\"facultyid\":\"C70230467\",\"primaryunitid\":9}},\"status\":[{\"grantid\":199,\"status\":\"Completed\",\"statuslabel\":\"Completed\",\"term\":\"Spring\",\"year\":2020,\"termid\":\"2019\\\/03\",\"listingorder\":4,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[],\"sort_date\":\"2020-08-31\"},{\"activityid\":221,\"fields\":{\"Title\":\"Biochemistry &amp; Mechanism of HECT E3 Ubiquitin Ligases\",\"Sponsor\":\"Carl J. and Anna Carlson Endowed Research Chair, Clark University\",\"Grant ID \\\/ Contract ID\":\"\",\"Award Date\":\"2015-08-01\",\"Start Date\":\"2015-08-01\",\"End Date\":\"2018-08-01\",\"Period Length\":3,\"Period Unit\":\"Year\",\"Indirect Funding\":0,\"Indirect Cost Rate\":null,\"Total Funding\":\"60000\",\"Total Direct Funding\":null,\"Currency Type\":\"USD\",\"Description\":\"\",\"Abstract\":\"&lt;p&gt;This three-year endowed research allowance from the Carlson School of Chemistry &amp; Biochemistry supports the on-going studies in Spratt Lab at Clark and allows for the purchase of equipment and training of graduate and undergraduate students examining HECT E3 ubiquitin ligases.&lt;\\\/p&gt;\",\"Number of Periods\":1,\"URL\":\"\"},\"facultyid\":\"C70230467\",\"funding\":{\"260\":{\"id\":260,\"grantid\":221,\"fundedamount\":\"60000\",\"yearfunded\":1,\"fundedtype\":\"Total\",\"currencytype\":\"USD\",\"startdate\":\"2015-08-01\",\"enddate\":\"2018-08-01\"}},\"coauthors\":{\"243\":{\"authorid\":243,\"grantid\":221,\"firstname\":\"Donald\",\"middleinitial\":\"E.\",\"lastname\":\"Spratt\",\"authortype\":\"PI\",\"percenteffort\":null,\"sameschoolflag\":1,\"facultyid\":\"C70230467\",\"primaryunitid\":9}},\"status\":[{\"grantid\":221,\"status\":\"Completed\",\"statuslabel\":\"Completed\",\"term\":\"Fall\",\"year\":2015,\"termid\":\"2015\\\/01\",\"listingorder\":4,\"completionorder\":6}],\"userid\":\"C70230467\",\"attachments\":[],\"sort_date\":\"2018-08-01\"}]","cu_faculty_title":"Professor, Chemistry","cu_faculty_department":"Chemistry","cu_faculty_affiliated_departments":"Chemistry, Biology","footnotes":""},"cu_faculty_group":[],"cu_faculty_department":[24],"cu_faculty_position":[],"class_list":["post-824","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>Don Spratt | 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\/don-spratt\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Don Spratt\" \/>\n<meta property=\"og:description\" content=\"Don Spratt is a Professor in the Gustaf H. Carlson School of Chemistry &amp; Biochemistry and the Director of STEM Summer Undergraduate Research Opportunities at Clark University. His NIH and MLSC funded research group focuses on the structural and mechanistic studies of the HECT E3 ubiquitin ligases and homeodomain transcription factors using biophysical approaches. 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