{"id":22087,"date":"2020-11-16T09:10:27","date_gmt":"2020-11-16T14:10:27","guid":{"rendered":"https:\/\/www.bu.edu\/chemistry\/?page_id=22087"},"modified":"2025-10-27T16:36:32","modified_gmt":"2025-10-27T20:36:32","slug":"biochemistry","status":"publish","type":"page","link":"https:\/\/www.bu.edu\/chemistry\/research\/areas\/biochemistry\/","title":{"rendered":"Biochemistry and Chemical Biology"},"content":{"rendered":"<h3>Biochemistry and Chemical Biology<\/h3>\n<div style=\"text-align: justify;\">The highly interdisciplinary research in the Department\u2019s biological chemistry area involves both experimental and computational projects. Studies focus on protein structure, nucleic acids, peptides and biomodel systems, and bioinorganic topics. Several faculty work in the bioanalytic area to develop methods with which to probe biological activity and detect biological molecules. In biophysical chemistry, research explores the connections between physical chemistry and the chemical function of biological molecules, including protein folding, nucleic acid structure, biological electron transfer, and macromolecular dynamics.<\/div>\n<h3>Core Faculty<\/h3>\n<table>\n<tbody>\n<tr>\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\"><img loading=\"lazy\" src=\"\/chemistry\/files\/2009\/06\/Allen_forweb.jpg\" alt=\"\" width=\"600\" height=\"900\" class=\"size-full wp-image-6178\" srcset=\"https:\/\/www.bu.edu\/chemistry\/files\/2009\/06\/Allen_forweb.jpg 600w, https:\/\/www.bu.edu\/chemistry\/files\/2009\/06\/Allen_forweb-200x300.jpg 200w\" sizes=\"(max-width: 600px) 100vw, 600px\" \/>\n<\/td>\n<td style=\"width: 70%; text-align: justify;\">\n<h3>Karen Allen<\/h3>\n<h4>Area: Enzyme mechanisms and macromolecular crystallography<\/h4>\n<p>Research in the Allen Group is concerned with diverse aspects of protein structure, function, and design. The laboratory employs a multidisciplinary approach involving state-of-the-art X-ray crystallography and spectroscopy, molecular modeling, enzymology, bioinformatics, and molecular biology to address fundamental problems at the interface of Enzymology and Structural Biology.\n<\/td>\n<\/tr>\n<tr>\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\"><img loading=\"lazy\" src=\"\/chemistry\/files\/2019\/11\/John-Caradonna.jpg\" alt=\"\" width=\"289\" height=\"385\" class=\"size-full wp-image-20858\" srcset=\"https:\/\/www.bu.edu\/chemistry\/files\/2019\/11\/John-Caradonna.jpg 289w, https:\/\/www.bu.edu\/chemistry\/files\/2019\/11\/John-Caradonna-225x300.jpg 225w\" sizes=\"(max-width: 289px) 100vw, 289px\" \/>\n<\/td>\n<td style=\"width: 70%; text-align: justify;\">\n<h3>John Caradonna<\/h3>\n<h4>Area: Bioinorganic chemistry<\/h4>\n<p>The Caradonna Group investigates non-heme iron metalloproteins, focusing on the chemistry of metalloenzyme active sites involved in biological oxidation reactions.  Using chemical, molecular biological, and biophysical (spectroscopic) techniques, their goal is to develop a global understanding of active site metal centers and the role of protein matrix in regulating, modulating, and tuning these properties.\n<\/td>\n<\/tr>\n<tr>\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\"><img loading=\"lazy\" src=\"\/chemistry\/files\/2019\/11\/Qiang-Cui-714x1024.jpg\" alt=\"\" width=\"714\" height=\"1024\" class=\"aligncenter size-large wp-image-20876\" srcset=\"https:\/\/www.bu.edu\/chemistry\/files\/2019\/11\/Qiang-Cui-714x1024.jpg 714w, https:\/\/www.bu.edu\/chemistry\/files\/2019\/11\/Qiang-Cui-209x300.jpg 209w, https:\/\/www.bu.edu\/chemistry\/files\/2019\/11\/Qiang-Cui-768x1101.jpg 768w, https:\/\/www.bu.edu\/chemistry\/files\/2019\/11\/Qiang-Cui.jpg 1071w\" sizes=\"(max-width: 714px) 100vw, 714px\" \/>\n<\/td>\n<td style=\"width: 70%; text-align: justify;\">\n<h3>Qiang Cui<\/h3>\n<h4>Area: Multi-scale Theory\/Computation in Chemistry and Biophysics<\/h4>\n<p>The Cui group develops and applies a broad range of theoretical and computational methods (QM\/MM, atomistic and coarse-grained simulations, continuum modeling) to study a diverse set of chemical and biological problems, focusing particularly on problems that implicate multiple length and temporal scales, such as enzyme catalysis, bioenergy\/signal transduction, biological membrane remodeling, macromolecular assembly and solid\/liquid interfaces. The group is engaged in close collaboration with many experimental groups on and off the BU campus.\n<\/td>\n<\/tr>\n<tr>\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\"><img loading=\"lazy\" src=\"\/chemistry\/files\/2010\/07\/Elliott_forweb.jpg\" alt=\"Professor Sean Elliott\" width=\"600\" height=\"900\" class=\"size-full wp-image-6236\" srcset=\"https:\/\/www.bu.edu\/chemistry\/files\/2010\/07\/Elliott_forweb.jpg 600w, https:\/\/www.bu.edu\/chemistry\/files\/2010\/07\/Elliott_forweb-200x300.jpg 200w\" sizes=\"(max-width: 600px) 100vw, 600px\" \/>\n<\/td>\n<td style=\"width: 70%; text-align: justify;\">\n<h3>Sean Elliott<\/h3>\n<h4>Area: Bioinorganic chemistry and metallobiochemistry<\/h4>\n<p>The Elliott Group uses Protein film voltammetry (PFV) to explore the electron transfer pathways and redox-dependent catalytic chemistry of complex metalloproteins such as sulfite reductase and multicopper oxidases. They also develop proteomic tools to enable probing the \u2018metallome\u2019 \u2014 a complete read-out of the metal-binding components of biological pathways. These experiments provide insights into the role of metal ions in biological chemistry.\n<\/td>\n<\/tr>\n<tr>\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\"><img loading=\"lazy\" src=\"\/chemistry\/files\/2009\/06\/ARROWS__0306__06-21-22-18-Edit-744x1024.jpg\" alt=\"\" width=\"744\" height=\"1024\" class=\"size-large wp-image-18771\" \/>\n<\/td>\n<td style=\"width: 70%; text-align: justify;\">\n<h3>Rosina Georgiadis<\/h3>\n<h4>Area: Analytical and Bioanalytical Chemistry<\/h4>\n<p>The Georgiadis Group research interests are the development of experimental tools to characterize biomolecular binding at surfaces and in solution, where binding partners may be proteins, oligonucleotides, small molecules, bioconjugates or nanoparticles.  Methods used to determine the kinetics and thermodynamics of binding and electric field effects on binding at interfaces include surface plasmon resonance (SPR) spectroscopy, surface acoustic wave (SAW) sensing, and fluorescence-based microscale thermophoresis (MST).\n<\/td>\n<\/tr>\n<tr>\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\"><img loading=\"lazy\" src=\"\/chemistry\/files\/2019\/11\/Mark-W.-Grinstaff.jpg\" alt=\"\" width=\"218\" height=\"300\" class=\"aligncenter size-full wp-image-20912\" \/>\n<\/td>\n<td style=\"width: 70%; text-align: justify;\">\n<h3>Mark Grinstaff<\/h3>\n<h4>Area: Macromolecular, bioinorganic, and biological chemistry<\/h4>\n<p>The Grinstaff Group pursues highly interdisciplinary translational research in biological and macromolecular chemistry.  Among their projects are novel dendrimers, \u201cbiodendrimers,\u201d for tissue engineering and biotechnological applications (corneal lacerations, delivery of anti-cancer drugs and DNA, and biodegradable scaffolds for cartilage repair). They also create \u201cinterfacial biomaterials\u201d that control biology on plastic, metal, and ceramic surfaces and  electrochemical-based sensors\/devices using conducting polymer nanostructures and specific DNA structural motifs.\n<\/td>\n<\/tr>\n<tr>\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\"><img loading=\"lazy\" src=\"\/chemistry\/files\/2019\/11\/Masha-Kamenetska.jpg\" alt=\"\" width=\"240\" height=\"300\" class=\"aligncenter size-full wp-image-20933\" \/>\n<\/td>\n<td style=\"width: 70%; text-align: justify;\">\n<h3>Masha Kamenetska<\/h3>\n<h4>Area: Single molecule detection, charge transport<\/h4>\n<p>The Kamenetska research group develops and uses novel single molecule detection and spectroscopy techniques to understand and control how the structure of the intermolecular interface affects function in biological and man-made devices. We are investigating DNA-protein and RNA-protein interactions to probe the structure and dynamics of these complexes. Current focus is on understanding the role of charge transport in nucleic acid function, nucleosome unwinding and DNA repair protein dynamics.\n<\/td>\n<\/tr>\n<tr>\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\"><img loading=\"lazy\" src=\"\/chemistry\/files\/2010\/07\/Liu_forweb.jpg\" alt=\"\" width=\"600\" height=\"900\" class=\"size-full wp-image-6288\" srcset=\"https:\/\/www.bu.edu\/chemistry\/files\/2010\/07\/Liu_forweb.jpg 600w, https:\/\/www.bu.edu\/chemistry\/files\/2010\/07\/Liu_forweb-200x300.jpg 200w\" sizes=\"(max-width: 600px) 100vw, 600px\" \/>\n<\/td>\n<td style=\"width: 70%; text-align: justify;\">\n<h3>Pinghua Liu<\/h3>\n<h4>Area: Signal transduction pathways in human innate-immune responses<\/h4>\n<p>The Liu Group focuses on the chemistry\/biology interface with emphasis on the chemical basis of pathogen and host interactions, as well as the chemical nature of the biological clock. These projects address two areas: mechanistic studies of the metallo-proteins using both biochemical and biophysical methods and identification of other components using genomic, proteomic, and biochemical approaches. Their goals are to develop broad-spectrum antibiotics, elucidate the mechanism of the isoprenoid biosynthesis pathway intermediate-triggered human innate-immune responses, and unravel the time recording mechanism inside the cell and its relationship to both aging and development.\n<\/td>\n<\/tr>\n<tr>\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\"><img loading=\"lazy\" src=\"\/chemistry\/files\/2010\/07\/Perlstein2.jpg\" alt=\"\" width=\"110\" height=\"164\" class=\"aligncenter size-full wp-image-6259\" \/>\n<\/td>\n<td style=\"width: 70%; text-align: justify;\">\n<h3>Deborah Perlstein<\/h3>\n<h4>Area: Biochemistry and Enzymology<\/h4>\n<p>The research of the Perlstein Group lies at the interface of chemistry and biology with a focus on bioinorganic chemistry. They are currently developing new projects that will use the tools of chemical biology, including biophysical techniques, enzymology, microscopy, and molecular biology, to understand iron-sulfur cluster containing proteins and bacterial cell division.\n<\/td>\n<\/tr>\n<tr>\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\"><img loading=\"lazy\" src=\"\/chemistry\/files\/2013\/07\/Reinhard_forweb.jpg\" alt=\"\" width=\"600\" height=\"900\" class=\"size-full wp-image-12555\" srcset=\"https:\/\/www.bu.edu\/chemistry\/files\/2013\/07\/Reinhard_forweb.jpg 600w, https:\/\/www.bu.edu\/chemistry\/files\/2013\/07\/Reinhard_forweb-200x300.jpg 200w\" sizes=\"(max-width: 600px) 100vw, 600px\" \/>\n<\/td>\n<td style=\"width: 70%; text-align: justify;\">\n<h3>Bj&ouml;rn Reinhard<\/h3>\n<h4>Area: Biophysical, physical, nano-bio, and materials chemistry<\/h4>\n<p>The <a href=\"http:\/\/www.bu.edu\/reinhardlab\/\" target=\"_blank\" rel=\"noopener noreferrer\">Reinhard Group<\/a> develops and characterizes functional nanomaterials. One area of interest is the development of biomimetic nanomaterials that can reconstitute functionalities of viruses for applications in drug delivery and therapeutics. A particular focus is on elucidating the fundamental mechanisms that determine the interactions between nanoparticles and cellular systems. A second area of interest is broadly in the area of photonic and plasmonic nanomaterials. These materials have unique properties that enable new and advanced sensing, imaging, and photocatalyis concepts. To implement these advancements, nanomaterials design and fabrication go along with the development of new spectroscopy and imaging technologies.\n<\/td>\n<\/tr>\n<tr>\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\"><img loading=\"lazy\" src=\"\/chemistry\/files\/2023\/08\/Son_2021.png\" alt=\"\" width=\"1500\" height=\"2100\" class=\"aligncenter size-full wp-image-24261\" srcset=\"https:\/\/www.bu.edu\/chemistry\/files\/2023\/08\/Son_2021.png 1500w, https:\/\/www.bu.edu\/chemistry\/files\/2023\/08\/Son_2021-214x300.png 214w, https:\/\/www.bu.edu\/chemistry\/files\/2023\/08\/Son_2021-731x1024.png 731w, https:\/\/www.bu.edu\/chemistry\/files\/2023\/08\/Son_2021-768x1075.png 768w, https:\/\/www.bu.edu\/chemistry\/files\/2023\/08\/Son_2021-1097x1536.png 1097w, https:\/\/www.bu.edu\/chemistry\/files\/2023\/08\/Son_2021-1463x2048.png 1463w, https:\/\/www.bu.edu\/chemistry\/files\/2023\/08\/Son_2021-429x600.png 429w\" sizes=\"(max-width: 1500px) 100vw, 1500px\" \/><\/td>\n<td style=\"width: 70%; text-align: justify;\">\n<h3>Minjung Son<\/h3>\n<h4>Area: Biophysical and physical chemistry<\/h4>\n<p>We aim to achieve systematic and selective control of the photophysics in biological and bioinspired light-harvesting systems towards improved energy production, such as photosynthetic light-harvesting proteins. We develop ways to engineer their conformational and\/or electronic structure using materials science and biochemical tools.<\/td>\n<\/tr>\n<tr>\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\"><img loading=\"lazy\" src=\"\/chemistry\/files\/2016\/03\/StraubPROFILE2.15-699x1024.jpg\" alt=\"\" width=\"699\" height=\"1024\" class=\"size-large wp-image-16253\" srcset=\"https:\/\/www.bu.edu\/chemistry\/files\/2016\/03\/StraubPROFILE2.15-699x1024.jpg 699w, https:\/\/www.bu.edu\/chemistry\/files\/2016\/03\/StraubPROFILE2.15-205x300.jpg 205w, https:\/\/www.bu.edu\/chemistry\/files\/2016\/03\/StraubPROFILE2.15.jpg 1678w\" sizes=\"(max-width: 699px) 100vw, 699px\" \/>\n<\/td>\n<td style=\"width: 70%; text-align: justify;\">\n<h3>John Straub<\/h3>\n<h4>Area: Biomolecular structure and dynamics<\/h4>\n<p>The Straub group focuses on the theoretical and computational modeling of biomolecular systems. Particular areas of interest include dynamics of energy transfer and signaling in proteins, the development of computational algorithms for folding, thermodynamics and phase changes in proteins and membranes, and the modeling of peptide and protein aggregation.\n<\/td>\n<\/tr>\n<tr>\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\"><img loading=\"lazy\" src=\"\/chemistry\/files\/2010\/07\/Tullius_forweb.jpg\" alt=\"\" width=\"600\" height=\"900\" class=\"aligncenter size-full wp-image-6295\" srcset=\"https:\/\/www.bu.edu\/chemistry\/files\/2010\/07\/Tullius_forweb.jpg 600w, https:\/\/www.bu.edu\/chemistry\/files\/2010\/07\/Tullius_forweb-200x300.jpg 200w\" sizes=\"(max-width: 600px) 100vw, 600px\" \/>\n<\/td>\n<td style=\"width: 70%; text-align: justify;\">\n<h3>Thomas Tullius<\/h3>\n<h4>Area: Biochemistry, genomics, bioinformatics<\/h4>\n<p>The <a href=\"http:\/\/dna.bu.edu\/tullius\/\" target=\"_blank\" rel=\"noopener noreferrer\">Tullius Group<\/a> focuses on developing and applying new chemical probe methods for determining the structure of DNA and RNA. They introduced the use of the hydroxyl radical as a high-resolution chemical footprinting reagent for nucleic acids. In recent years the Tullius Group has focused on extending the hydroxyl radical footprinting method to the whole-genome scale, by using high throughput DNA sequencing to analyze the experiment. Current projects include the development of a new method for determining the tertiary structure of all RNA molecules in a cell, in one experiment.\n<\/td>\n<\/tr>\n<p><!--\n\n\n<tr>\n\n\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\"><img loading=\"lazy\" src=\"\/chemistry\/files\/2019\/12\/Arturo-Vegas-683x1024.jpg\" alt=\"\" width=\"683\" height=\"1024\" class=\"aligncenter size-large wp-image-20979\" srcset=\"https:\/\/www.bu.edu\/chemistry\/files\/2019\/12\/Arturo-Vegas-683x1024.jpg 683w, https:\/\/www.bu.edu\/chemistry\/files\/2019\/12\/Arturo-Vegas-200x300.jpg 200w, https:\/\/www.bu.edu\/chemistry\/files\/2019\/12\/Arturo-Vegas-768x1152.jpg 768w\" sizes=\"(max-width: 683px) 100vw, 683px\" \/>\n<\/td>\n\n\n\n\n<td style=\"width: 70%; text-align: justify;\">\n\n\n<h3>Arturo Vegas<\/h3>\n\n\n\n\n<h4>Area: Organic synthesis, biological chemistry, and drug delivery<\/h4>\n\n\nThe Vegas group pursues general and systematic approaches to developing targeted therapeutic carriers for the treatment of multiple human diseases. Projects in the lab are focused on developing novel chemical tools, materials and approaches for targeting therapeutics to diseased tissues, with an emphasis on cancer and diabetes. For cancer, the primary focus will be developing conjugate and nanoparticle based approaches that control the physiological distribution and uptake of therapeutic molecules to tumors and use of materials to immunomodulate the tumor microenvironment. For diabetes, our focus will be selective destruction or functional blocking of cells responsible for the underlying type 1 autoimmunity.\n<\/td>\n\n<\/tr>\n\n\n--><\/p>\n<tr>\n<td style=\"text-align: center; width: 20%; vertical-align: middle;\">]<img loading=\"lazy\" src=\"\/chemistry\/files\/2010\/07\/Whitty_forweb.jpg\" alt=\"\" width=\"600\" height=\"900\" class=\"size-full wp-image-6208\" srcset=\"https:\/\/www.bu.edu\/chemistry\/files\/2010\/07\/Whitty_forweb.jpg 600w, https:\/\/www.bu.edu\/chemistry\/files\/2010\/07\/Whitty_forweb-200x300.jpg 200w\" sizes=\"(max-width: 600px) 100vw, 600px\" \/>\n<\/td>\n<td style=\"width: 70%; text-align: justify;\">\n<h3>Adrian Whitty<\/h3>\n<h4>Area: Biochemistry and bioorganic chemistry<\/h4>\n<p>The Whitty Group research centers around reversible noncovalent interactions involving proteins: how they regulate function in complex biological systems such as whole cells, and how they can be exploited in the development of artificial agonists and antagonists for use as protein or small molecule drugs. Their perspective is primarily quantitative and mechanistic, aiming to understand the macroscopic functional behavior of the system in terms of the structures, properties and interactions of the molecules involved.\n<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n","protected":false},"excerpt":{"rendered":"<p>Biochemistry and Chemical Biology The highly interdisciplinary research in the Department\u2019s biological chemistry area involves both experimental and computational projects. Studies focus on protein structure, nucleic acids, peptides and biomodel systems, and bioinorganic topics. Several faculty work in the bioanalytic area to develop methods with which to probe biological activity and detect biological molecules. In [&hellip;]<\/p>\n","protected":false},"author":10766,"featured_media":0,"parent":20524,"menu_order":1,"comment_status":"closed","ping_status":"closed","template":"","meta":[],"_links":{"self":[{"href":"https:\/\/www.bu.edu\/chemistry\/wp-json\/wp\/v2\/pages\/22087"}],"collection":[{"href":"https:\/\/www.bu.edu\/chemistry\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www.bu.edu\/chemistry\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www.bu.edu\/chemistry\/wp-json\/wp\/v2\/users\/10766"}],"replies":[{"embeddable":true,"href":"https:\/\/www.bu.edu\/chemistry\/wp-json\/wp\/v2\/comments?post=22087"}],"version-history":[{"count":44,"href":"https:\/\/www.bu.edu\/chemistry\/wp-json\/wp\/v2\/pages\/22087\/revisions"}],"predecessor-version":[{"id":25467,"href":"https:\/\/www.bu.edu\/chemistry\/wp-json\/wp\/v2\/pages\/22087\/revisions\/25467"}],"up":[{"embeddable":true,"href":"https:\/\/www.bu.edu\/chemistry\/wp-json\/wp\/v2\/pages\/20524"}],"wp:attachment":[{"href":"https:\/\/www.bu.edu\/chemistry\/wp-json\/wp\/v2\/media?parent=22087"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}