University of Maryland, Baltimore County (UMBC), Department of Chemistry and Biochemistry and affiliated faculty; *University of Maryland, Baltimore (UMB), Institute for Human Virology; **UMBC, Institute of Fluorescence
RICHARD L. KARPEL, Acting Chair
BRIAN CULLUM, Graduate Program Director
BUSH, C. ALLEN, Ph.D., University of California, Berkeley; Chemical structure and three-dimensional conformation of complex carbohydrates of glycoproteins and polysaccharides of the cell surface using biophysical methods such as NMR spectroscopy, circular dichroism and molecular modeling
FISHBEIN JAMES C., Ph.D., Brandeis University; Mechanisms of organic reactions in aqueous solutions: generation and study of reactive intermediates, particularly those involved in nitrosamine and nitrosamide carcinogenesis and chemical toxicology
GEDDES, CHRISTOPHER,** Ph.D., University of Wales;Methods and applications of fluorescence spectroscopy and imaging techniques to the life sciences; with particular emphasis on bacterial, pathogen and virus detection
KARPEL, RICHARD L., Ph.D., Brandeis University; Nucleic acid helix-destabilizing proteins, protein-nucleic acid interactions and retroviral structural proteins
LACOURSE, WILLIAM R., Ph.D., Northeastern University; Development and application of hydrodynamically controlled electrochemical detection systems
LIEBMAN, JOEL F., Ph.D., Princeton University; Strained organic compounds and their energetics, gaseous ions, noble gas and fluorine chemistry, mathematical and quantum chemistry
LU, WUYUAN,* Ph.D., Purdue University; Protein engineering via total chemical protein synthesis
SELEY, KATHERINE L., Ph.D., Auburn University; Design and synthesis of nucleoside/ nucleotide and hetero-cyclic enzyme inhibitors for use as medicinal agents
SUMMERS, MICHAEL F., Ph.D., Emory University; Howard Hughes Associate Medical Investigator; Elucidation of structural, dynamic and thermodynamic features of metallo-biomolecules using advanced multi-dimensional and multi-nuclear NMR methods
WANG, LAI-XI,* Ph.D., Shanghai Institute of Organic Chemistry; Chemoenzymatic synthesis of oligosaccharides, glycopeptides and glycoproteins
ARNOLD, BRADLEY R., Ph.D., University of Utah; Physical chemistry and applications of time-resolved polarized spectroscopy
CULLUM, BRIAN M., Ph.D., University of South Carolina; Development of optical sensors and optical-sensing techniques for biomedical and environmental research
KELLY, LISA A., Ph.D., Bowling Green University; Mechanistic investigations of visible-light-induced redox reactions using laser flash photolysis techniques, with particular emphasis on developing synthetic chemical assemblies that efficiently undergo chemical redox reactions with biological substrates
SMITH, PAUL J., Ph.D., University of Pittsburgh; Bio-organic and physical organic chemistry, biomimetic catalysis, DNA structure and DNA binding by small molecules
ALLEN, MARK, Ph.D., Montana State University; Biotemplated material synthesis for enery applications. Using bio-engineering and basic molecular biology our lab develops multifunctional peptide units that serve as templates for coordinating and mineralizing functional materials with emphases on energy storage and catalysis
AN, SONGON, Ph.D., University of Minnesota Ė Twin Cities; Cellular biochemistry and enzymology investigating regulatory mechanisms of metabolic macromolecular complexes; transient protein-protein interactions and cellular enzyme kinetics, via fluorescence live-cell imaging and chemical biology techniques
DANIEL, MARIE-CHRISTINE, Ph.D., University of Bordeaux, France 2003; virus-nanoparticle complexes, supramolecular chemistry
GARCIN, ELSA D., Ph.D., Universite Joseph Fourier, Grenoble (France); Structure function relationship studies of protein targets relevant to cardiovascular diseases via combined biochemical, biophysical and structural analysis
PTASZEK, MARCIN, Ph.D., Jagiellonian University, Krakow (Poland); Develop of new fluorescent probes for in vivo imaging, and their applications for cancer diagnosis
THORPE, IAN F., Ph.D., The Scripps Research Institute; Studies of how small molecules allosterically inhibit the polymerase in Hepatitus C virus and rational design of cellulase enzymes for increased efficiency using theoretical and molecular simulation models WHITE, RYAN J., Ph.D., University of Utah; Development of electrochemical, biological and chemical senors at the naoscale that probe materials and biological systems with unprecedented temporal and spatial resolution. Analytical research utilizing nanoscience, biomolecular engineering and electrochemistry
The Department of Chemistry and Biochemistry at UMBC offers graduate programs in the disciplines of analytical, biochemical, organic, inorganic and physical chemistry leading to the doctoral degree in Chemistry (including Biochemistry). The diversity of faculty research represented in the program enables students to combine the study of energetics, structure and dynamics of chemical systems with their application to problems in the biological sciences. A masterís in these same chemical disciplines is also available through the Department of Chemistry and Biochemistry at UMBC. (See also joint programs in Biochemistry, Molecular and Cell Biology and Marine-Estuarine Environmental Science.)
All students enrolled in the M.S. and Ph.D. programs are required to complete a core program of study consisting of four out of a selection of 400- and 600-level courses in all areas. This core can be completed during the first year of graduate school.
Doctoral candidates are expected to enroll in other advanced courses in their area of specialization in addition to the core program of courses. Completion of a minimum of three additional courses (nine credit hours) at the 600-level or higher, along with 12 credit hours of CHEM 899: Dissertation Research, is required. A minimum of two semesters of teaching is required of all doctoral candidates.
A candidate for the masterís degree must complete 30 credit hours of course work (including the core program), of which 18 credits must be at the 600-level or higher. The program is flexible enough to meet a wide range of student interests. Students electing to do a masterís thesis will complete six credit hours of CHEM 799: Masterís Thesis Research. A non-thesis option, in which additional course work is undertaken in lieu of the thesis, also may be selected. In this case, the student will obtain some experience in research by completing CHEM 600: Advanced Laboratory Projects.
In either program, the remaining courses and seminars may be taken in areas of interest to the student(with approval of their advisor), including the biological sciences, physics, mathematics, chemistry and chemical engineering. Prior to registration for the first semester of graduate study, each new graduate student will meet with a member of the graduate committee who will assist in planning and implementing the degree program until a research advisor is selected.
Each doctoral student will begin a laboratory rotation in the fall semester and select a research advisor prior to the start of the second semester of study. When a student elects to do dissertation research with a particular faculty member, that faculty member becomes the studentís research advisor. During the first year of graduate study, masterís students who select the thesis option will consult individually with the members of the faculty to discuss the choice of a thesis topic. If a thesis advisor is chosen, the advisor will become the studentís counseling major advisor. All entering M.S. and Ph.D. students are asked to take placement examinations. Students whose background is deficient in specific areas will be required to enroll in appropriate undergraduate courses and obtain a grade of ďBĒ or better. Students excelling on those examinations may be exempted from specific core courses.
For all masterís students, a final oral examination will be arranged in accordance with the procedures of the department. This examination will follow completion of formal course work and the submission of either the masterís thesis or, in the case of the non-thesis option, a scholarly paper indicating the studentís familiarity with an area of modern chemical research. In addition to course requirements, doctoral students must successfully complete the four levels of progression toward the Ph.D. degree:
- Literature Review
- Advancement-to-Candidacy Examination
- Original Research Proposal
- Final Dissertation Defense
In each of these steps, the student is evaluated by a committee consisting of at least four program faculty,(three of whom are from the studentís sub-discipline, one of whom is outside this sub-discipline)and one member from outside the program. The members of this committee are chosen by the studentís research advisor in consultation with the student. To help monitor the studentís progress toward the Ph.D. degree, the committee should vary as little as possible. There is no language requirement for the M.S. or Ph.D. degrees. The Department of Chemistry and Biochemistry has a brochure that describes its graduate programs and the research interests of its faculty. For a copy of the brochure, or for specific information on the M.S. and Ph.D. programs in chemistry, contact the department office, 866-743-8622. A frequently updated version of the brochure may be accessed via the UMBC homepage at www.umbc.edu/chem-biochem. The Graduate Student Handbook is also available from the department office.
Program Admission Requirements
Most students entering the M.S. or Ph.D. programs will be expected to have majored in chemistry, or biochemistry, but applications are welcome from students who majored in other fields, provided their records indicate the ability to complete the program successfully. The desired undergraduate background includes courses in organic, analytical and physical chemistry; physics; calculus; and some work in the biochemical sciences. Scores on the Graduate Record Examinations (GRE) (verbal, quantitative and analytical tests) are required. The GRE Advanced Chemistry Test is strongly recommended.
Facilities and Special Resources
UMBC students are offered hands-on access to an extensive array of tools for modern chemical and biochemical research. The departmentís specialized research instrumentation includes calorimetry, chromatography, stopped-flow and temperature-jump kinetics, transient laser spectroscopy (including nano-second laser flash photolysis, pico-second and femto-second pump-probe and picosecond fluorescence systems), nuclear magnetic resonance spectroscopy (including one 200-, one 300-, one cryoprobe-equipped 500-, two 600- and one 800-MHz instruments), X-band CW electron paramagnetic resonance spectrometry, circular dichroism, X-ray diffraction, infrared spectroscopy, atomic absorption and gas chromatography mass spectrometry and both a 7 and 12 Tesla Fourier transform ion cyclotron resonance mass spectrometer apparatus, as well as extensive molecular modeling and computational chemistry facilities.
The department also hosts a BiochemistryMolecular Characterization and Analysis Complex (MCAC), which specializes in the analysis of environmental and biological molecules (e.g., biopolymers, peptides and glycoproteins). In addition to TOF/FT, a laser desorbtion mass spectrometer and both 500- and 600-MHz NMRs, this center houses one of the few tandem mass spectrometers located in academic institutions worldwide. The Howard Hughes Medical Institute suite houses a second 600- and an 800-MHz NMR instrument, both of which are used for high-dimensional studies of HIV proteins, metallo-biomolecules and macro-molecular interactions. The Albin O. Kuhn Library and Gallery contains more than 2,500 volumes of chemistry and biochemistry texts and subscribes to more than 150 chemistry and biochemistry periodicals.
Students completing the M.S. or Ph.D. degree programs at UMBC have continued their graduate or post-doctoral training at such competitive and prestigious institutions as the Johns Hopkins Medical and Graduate Schools and MIT, Harvard, Cornell, Columbia, Brandeis and Georgetown universities and have gone on to be faculty at prestigious universities across the country. Program graduates have also gone on to be leaders in the government and industrial workforce, finding employment with local, national and international organizations such as the U.S. D.o.D., NIH, the FDA, Ciba-Geigy, DuPont-Merck, Eastman Kodak-France, Glaxo Smith Kline, Proctor & Gamble, the U.S. Patent Office, etc.
Support is available on a competitive basis to students accepted into the program. Qualified first-year students are usually offered teaching assistantships. Research assistantships are often available for students actively engaged in thesis research. In addition, students are encouraged to apply for nationally awarded graduate fellowships. Student loans are available through the Office of Financial Aid.
Fellowship Opportunities at the Interface of Chemistry and Biology
UMBC recently has authorized a limited number of fellowships for incoming graduate students who are interested in both the areas of chemistry and biology. These fellowships aim to prepare students for the challenges of the 21st century, which will reward those who have expertise in more than one area of science. Even now, those scientists who can bridge the gap between biology and chemistry are in high demand in such areas as the pharmaceutical industry. Synthetic chemists who are knowledgeable about metabolism and biologists who understand the physical principles governing the interactions between macro-molecules are widely sought after.
Fellowship recipients will obtain their Ph.D. degree in an area of the chemical or the biological sciences, but with an additional focus in the other discipline. Each course of study will be individually tailored to take into account studentís strengths and interests, but all will include coursework at an advanced level in the biological sciences and chemistry, as well as biochemistry. In addition, students will carry out research rotations in the laboratories of faculty members from both disciplines and will attend seminars from both departments.
Chemical and Statistical Thermodynamics 
Intended for advanced undergraduates and first-year graduate students, this course is a treatment of chemical and statistical thermodynamics at a more sophisticated level than that encountered in CHEM 301/302. Emphasis is placed on the use of thermodynamic data available in chemical literature and experimental methods of obtaining these data. (Spring)
Inorganic Chemistry 
Basic theoretical concepts of inorganic chemistry, including a study of the periodic table, its elements, and their physical and chemical properties. Several theories of bonding are discussed, as well as the mechanisms of inorganic reactions, coordination chemistry and the chemistry of transition metals. (Fall)
Comprehensive Biochemistry I 
The first semester of a two-semester sequence providing a thorough introduction to modern biochemical principles. Major topics include enzyme kinetics and structures and the properties of proteins, nucleic acids, carbohydrates and lipids. (Fall)
Advanced Laboratory Projects [1-3]
This course is intended primarily for students selecting the non-thesis option for the M.S. degree. Students will be assigned individually supervised laboratory projects designed to increase familiarity with modern experimental techniques in chemistry. Note: In most cases, a single project will be undertaken during any given semester. A detailed account of work completed will be required. Prerequisite: Consent of instructor.
Current Topics in Chemistry [1-4]
A discussion of specialized topics in rapidly evolving areas of chemistry. The format of the course will be tutorial and may include varied topics such as applications of mass spectrometry in biochemistry and pharmacology or advanced NMR techniques. Prerequisite: Consent of instructor.
Introduction to Laboratory Research [1-3]
The purpose of this course is to familiarize graduate students with the different areas of research within the Department of Chemistry and Biochemistry, to expand their knowledge of experimental techniques and to provide the basis for a more informed selection of an advisor for thesis research. Note: For the joint biochemistry program, a student enrolling in the course will work for periods of about six weeks in the laboratories of three faculty members, at least one of whom should be engaged in an area of research different from the studentís preferred area of specialization.
Advanced Inorganic Chemistry Laboratory 
The core skills that will be emphasized in the course are anaerobic synthesis and advanced characterization methods. These methods will be applied to inorganic complexes important in biological/medicinal inorganic chemistry and nanomaterials. The course aims to combine traditional inorganic chemistry concepts/methods with areas of inorganic chemistry not typically covered in lower-level courses.
Bio-Inorganic Chemistry 
The functions of metals in biology and medicine are presented, with emphasis on the structural and catalytic properties of metal centers in metallo-proteins. Topics include catalysis, metallo-enzyme mechanisms, inorganic co-factors and co-enzymes and metal chemotherapeutic agents. Prerequisite: CHEM 405 or consent of instructor.
Special Topics in Theoretical Chemistry 
Discussions of current approaches to problems in theoretical chemistry will be presented in the form of lectures and seminars. Topics to be discussed may include molecular orbital theory, statistical mechanics of non-ideal systems, cooperative systems, phase transitions and critical phenomena, non-equilibrium thermodynamics and rate theory, scattering theory and molecular spectra. Prerequisite: Consent of instructor.
Statistical Mechanics and Theory of Rate Processes 
Introduction to statistical mechanics and theoretical aspects of absolute reaction rate theory. Statistical definition of entropy; compounding of systems; combinatorial problems; the methods of Gibbs; quantum statistics; partition functions; applications in equilibrium states of gases, solids and liquids; and partition formulation of the theory of absolute reaction rates. Prerequisite: Consent of instructor.
Chemistry of Proteins 
An advanced treatment of the chemistry of proteins and protein-containing supramolecular structures. The topics include isolation and purification of proteins, structure of proteins and relation of structure to biological function. Prerequisites: BIOL 430, CHEM 437 or equivalent and consent of instructor.
Advanced Biochemistry 
The topics presented would not normally be covered in any other biochemistry courses and may include an advanced treatment of enzyme kinetics, with emphasis upon two substrate systems, allosteric control mechanisms, replication and transcription, and the biochemistry of specialized tissues. Prerequisite: Consent of instructor.
Biochemistry of Nucleic Acids 
A survey of nucleic acid structure and function, with emphasis on chemical aspects. Topics will include DNA and RNA structure, packaging of nucleic acids, chemical and physical properties of nucleic acids, proteins and enzymes of DNA replication, fidelity of nucleic acid synthesis, biochemistry of DNA recombination, enzymology of transcription and RNA processing. Prerequisite: Consent of instructor.
Biochemistry of Complex Carbohydrates 
This course will address the structure and function of the carbohydrates of glycoproteins, glycolipids, proteoglycans and bacterial polysaccharides. Topics also will include carbohydrates as informational macro-molecules and decoding by lectins, biosynthesis, structure, engineering of glycoproteins, bacterial adhesion and virulence and tumor antigens. Prerequisite: CHEM 437 or equivalent.
Comprehensive Biochemistry II 
The student will be required to attend the undergraduate lecture course in biochemistry (CHEM 438: Comprehensive Biochemistry), which covers metabolic pathways and selected topics in nucleic acid and membrane biochemistry. In addition, the student will be assigned reading in the research literature in one or more of the above areas and be required to present a seminar or write a paper based on this reading. Note: This course is intended primarily for first-year graduate students who have completed CHEM 437: Comprehensive Biochemistry I.
Special Topics in Molecular Structure 
Discussions of the major physical methods for determining of molecular structure will be presented. Emphasis will be placed on the application of theoretical principles to experimental problems and to computational methods required for interpretation of data. Topics discussed may include X-ray, electron and neutron scattering, molecular spectroscopy (infrared, ultraviolet and microwave), nuclear magnetic and electron spin resonance, dipole moment determination and dielectric relaxation. Prerequisite: Consent of instructor.
Physical Chemistry of Macro-molecules 
Introductory course with emphasis placed on developing broad general concepts applicable to the study of all types of macro-molecules, e.g. synthetic and biological. Topics considered include determination of molecular weight distributions, and conformational properties of high polymers; thermodynamics; and transport properties of polymersolutions, polyelectrolytes and polymerization processes. Techniques such as sedimentation analysis, light scattering, osmometry and viscometry will be discussed. Prerequisites: Consent of instructor.
Physical Biochemistry 
Structural determination of proteins and nucleic acids in the solid state and in solution. Transitions between and stability of secondary and tertiary structure. Ligand binding and association processes. Interpretation of spectra, titration curves, multi-component equilibria, hydrodynamic properties and fluorescence polarization. Prerequisites: CHEM 437 or equivalents.
Molecular Spectroscopy and Biopolymers 
Team-taught course covering theory and applications of advanced spectroscopic techniques used to study the structure and function of bio-macro-molecules (polysaccharides, DNA, co-enzymes and co-factors). Aspects of modem Fourier transform NMR, including one- and two-dimensional methods (COSY, NOESY and HOHAHA) will be presented. Principles of mass spectrometry and examples of the potential, limitations and applications of electron impact; desorption ionization, high-resolution tandem mass spectrometry; and interfaced chromatography/mass spectrometry will be discussed. Theory and applications of other spectroscopic techniques, including molecular vibrational (Raman, resonance Raman and infrared), electron spin resonance (ESR) and laser fluorescence spectroscopies also will be presented. Prerequisite: Consent of instructor.
Molecular Modeling 
Survey of theoretical methods for simulation of biopolymer conformation. Force fields, energy maps, energy minimization and molecular dynamics simulation. Influence of solvents. Applications to proteins, nucleic acids, etc. Laboratory section will emphasize practical calculations on biopolymers and use of databases of structural biochemistry. Prerequisite: CHEM 437 or equivalent or consent of the instructor.
Chemistry of Heterocyclic Compounds 
An in-depth survey of the properties, reactions and synthesis of heterocyclic compounds containing the heteroatoms of oxygen, sulfur and/or nitrogen. The course will consist of lectures based on readings from monographs and current literature. Prerequisite: Consent of instructor.
Mechanisms of Organic Reactions 
Advanced general treatment of the study of organic reaction mechanisms, with emphasis on developing of broad principles governing various organic reactions. Description of metastable intermediates, such as carbonium ions, carbanions, carbenes and free radicals; kinetic effects in relation to structure; conformational analysis and stereochemistry.
Physical Organic Chemistry 
Introduction to theoretical aspects of organic chemistry. Molecular orbital approximations, linear free-energy relationships, general theory of acid-base catalysis, medium effects and isotope effects. Prerequisites: CHEM 451 and consent of instructor.
Organic Chemistry of Nucleic Acids 
A survey of organic chemical principles governing structure, properties and reactions of nucleic acids, including synthesis of nucleic acid bases, nucleosides, nucleotides and poly-nucleotides and their important synthetic analogs possessing anti-viral and anti-tumor properties. Study of reactivity of nucleic acid building blocks, including addition and substitution reactions, ring openings and rearrangements, hydrolysis of glycosidic and phosphodiester bonds and photochemical reactions. Study of primary structure, acid-base property, tautomerism and conformation of nucleic acids. Review of secondary structure, base-pairing and stacking interactions, helical structure, stability, conformation, denaturation, renaturation and cross-linking. Prerequisite: Consent of instructor.
Organic Synthetic Methodology 
A survey of the basic principles of reactivity, reactions and strategies in organic synthesis. The course will focus on reactions leading to new bond formation, functional group transformation and the combination of these reactions in the synthesis of complex organic molecules. Lectures will be based on readings from monographs and current literature. Prerequisite: Consent of instructor.
Introduction to Biomedicinal Chemistry 
A survey of (a) principles and methods of drug design, including modern rational approach aided by computers, disease models, natural products, analogue synthesis and pharmacophore identification; (b) physio-chemical principles of drug action, including solubility; partition co-efficients; surface interactions; stereo-chemical, electronic and quantum chemical factors; chemical bonding; and quantitative structure activity relationships (QSAR); (c) receptor concept of drug action, including nature, definition, characterization, models and classical theories of receptor function; (d) mechanisms of drug action, including enzyme stimulation, inhibition and regulation; (e) drug distribution, metabolism and inactivation, including bioavailability, biotransformations, chemical and metabolic stability; pharmaco-kinetic variability and design of pro-drugs; (f) case studies selected from a list of anti-tumor, analgetic, anti-microbial, anti-cholinergic, anti-adrenergic, psychoactive and cardiovascular drugs; and (g) current status and future impact in drug development, including protein therapeutics, gene therapy, anti-sense drugs, cytokines and drug resistance. Prerequisite: Consent of instructor.
Total Synthesis of Natural Products 
The course will cover the total syntheses of selected natural products from animal, plant, marine, bacterial and fungal sources, including vitamins, alkaloids, hormones, terpenoids and antibiotics. Both historically significant total syntheses of landmarks, such as those of cholesterol, morphine, strychnine and vitamin B12, and the more modern total syntheses, such as those as taxol, bleomycin and enediyne antibiotics, will be elaborated. Students who opt to take the course for graduate credits (CHEM 657) will be required to write an additional term paper and/or make an oral presentation on the total synthesis of a selected natural product.
Special Topics in Analytical Chemistry 
A course of lectures and seminars devoted to modern methods in analytical chemistry. Two of the following topics will be considered: instrumental methods in spectroscopic analysis, scattering and diffraction methods, electro-analytical and polaro-graphic techniques, chromatography, separation and purification methods and tracer methods. Readings from current literature will be the basis of both lectures and seminars. Prerequisite: Consent of instructor.
Advanced Instrumental Methods of Analysis 
A lecture/laboratory course devoted to the theory, instrumentation and application of modem electro-chemical, spectroscopic and chromatographic techniques. Advantages and limitations of different instrumental methods are discussed using selected topics of environmental, clinical and toxicological analyses. Journal articles will be used to review recent advances and new trends in developing analytical techniques. Laboratory experiments may include polarography and pulse voltammetry, anodic stripping analysis, potentiometry with ion selective electrodes, flame and electro-thermal atomic absorption, UV-VIS spectrophotometry, Raman spectroscopy, electrophoresis, capillary gas chromatography and high-performance liquid chromatography (HPLC) and gas chromatography/mass spectroscopy. (Spring) Prerequisite: Consent of instructor.
Analytical Spectroscopy 
An advanced course in spectroscopic methods of qualitative and quantitative analysis, with emphasis on instrumental design, construction and operation. Topics will include atomic spectroscopy, light scattering and electronic and vibrational molecular spectroscopy. The role of lasers in modem spectroscopic methods will be explored.
Analytical Separations 
An advanced course in separation science, with emphasis on chromatographic techniques. This course will cover the theory of chemical separations, physical description and operation of various chromatographic instruments and general application of these techniques. Readings from current literature will supplement the lectures.
Electronics for Chemists 
A lecture-lab course designed to introduce chemists to a wide range of electronic principles from electron theory to digital computer technology. This course will cover alternating and direct current electronics, semi-conductor technology and signal processing. Emphasis will be placed on circuits and electronic applications commonly found in chemical research laboratories.
Special Topics in Dynamics and Mechanisms 
Discussions of the major methods and approaches to the study of chemical kinetics and other rate processes as applied to the elucidation of mechanisms of organic, inorganic and biochemical reactions. One or two of the following topics may form the basis of a semesterís work in this course: rapid-reaction techniques; stopped-flow, pressure and temperature jump methods; ultrasonics; inorganic reaction mechanism solvation; electron and proton transfer and substitution reactions; biocatalysis inhibition activation and allosteric effects; kinetics of structural transitions and phase transformation; gas-phase kinetics and heterogeneous catalysis. Prerequisite: Consent of instructor.
Enzyme Reaction Mechanisms 
The mechanism of enzyme action will be examined, with emphasis on the following topics: three-dimensional structure of enzymes, chemical catalysis, methods of determining enzyme mechanisms, sterochemistry of enzymatic reactions, detection of intermediates, affinity labels and suicide inhibitors, transition state analogs, energy relationships, evolutionarily ďperfectĒ enzymes, genetic engineering and enzymes and use of binding energy in catalysis. Instruction will be in both lecture and seminar format, with emphasis on recent literature. Prerequisites: CHEM 437 or consent of instructor. Note: CHEM 651 recommended.
Seminar in Biophysical Chemistry 
A series of lectures and weekly seminars dealing with current developments in the field of biophysical chemistry.
Special Topics in Biochemistry 
A series of weekly lectures and seminars dealing with topics of current research interest in the field of biochemistry. A single area in which advances of major significance have been made may be chosen.
Special Topics in Chemistry [1-4]
A series of weekly lectures and seminars dealing with recent or current important developments in chemistry. A single area in which advances of major significance have been made, or a given term, e.g., physical, organic or inorganic chemistry, will be selected.
Chemistry Seminar 
A series of weekly seminars devoted to a wide range of topics encompassing current literature in all fields of chemistry. Note: Each student will be required to present an extensive written paper based on the seminar and on collateral readings from current literature. Enrollment will be limited to ensure each participating student has an opportunity to present at least one major seminar. Prerequisite: Consent of instructor.
Research Tutorial in Chemistry 
Intensive tutorial seminar on current topics of research actively pursued by the faculty member directing the course.
Biochemistry/Chemistry Seminar 
This core course will be given to first- and second-year graduate students. A varied background in the biochemistry/chemistry current research fields will be presented. Note: Students will be required to attend eight seminars in the semester either at the UMB Department of Biochemistry and Molecular Biology or the UMBC Department of Chemistry and Biochemistry. Also listed as GPLS 713 (UMB).
Masterís Thesis Research [2-9]
Masterís thesis research conducted under the direction of a faculty member. Recommended: Six credit hours are required for the masterís degree.
Pre-Candidacy Doctoral Research [3-9]
Research on doctoral dissertation conducted under the direction of a faculty advisor before candidacy.
Doctoral Dissertation Research 
Research on doctoral dissertation conducted under the direction of a faculty advisor. Note: A minimum of 18 credit hours are required for the doctoral degree.