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| Biochemistry and Biophysics (School of Science) |
| BCBP-2900 Research in Biochemistry/Biophysics Hands-on research in a faculty member’s research laboratory. Prerequisite: permission of instructor. Offered each term. 3 to 4 credit hours, 9 to 12 contact hours |
| BCBP-2930 Out-of-Classroom Experience in Biochemistry/Biophysics Credit to be given for an out-of-classroom experience related to biochemistry and/or biophysics (BCBP) having intellectual content relevant to the student’s educational or career goals, subject to approval of a written proposal and a final written report. The adviser (for BCBP majors) or, with permission, any BCBP faculty member may serve as evaluator. For each out-of-classroom experience a student may register only once. 1 to 4 credit hours |
| BCBP-2940 Readings in Biochemistry/Biophysics Independent study of selected readings in the fields of biochemistry and biophysics, supervised by a faculty member. Prerequisite: permission of instructor. Offered each term. 1 to 4 credit hours |
| BCBP-2990 Research Thesis Independent research, supervised by a faculty member, culminating in a written thesis. Prerequisite: permission of instructor. Offered each term. 3 to 4 credit hours, 9 to 12 contact hours |
| BCBP-4210 Biophysical Methods Topics covered will include electron microscopy of ordered samples, structural databases, hydrodynamics of biological macromolecules, viscosity, sedimentation, translational and rotational diffusion, chromatography, conductance, dielectrophoresis, dynamic light scattering, flow and electric birefringence, and electrophoresis. Also water as a solvent, polyelectyrolytes, and Debye-Huckel theory. (Students cannot obtain credit for both this course and BCBP-6210.) Prerequisite: CSCI-1100, BIOL-2120, CHEM-2440, and PHYS-1100 or equivalents. Spring term odd-numbered years. 4 credit hours |
| BCBP-4310 Genetic Engineering Case studies on the effect of genetic engineering on medicine, agriculture, biology, forensics, and various other areas of technology. Each week a set of assigned readings will be discussed. Some of the topics to be covered are vaccines, biomolecular computing and electronics, paleontology, ecology, bioremediation, and polymers. (Students cannot obtain credit for both this course and BCBP- 6310.) Prerequisite or corequisite: BCBP-4760 and BIOL-4620, or permission of instructor. Fall term, odd-numbered years. 4 credit hours |
| BCBP-4710 Biochemistry Laboratory Major principles of biochemistry are illustrated as students purify and analyze specific proteins. Experience is obtained with various techniques including tissue extraction, chromatography, ultracentrifugation, spectrophotometric analysis, and electrophoresis. The course includes extensive hands-on laboratory work, as well as the writing of in-depth reports. (Students cannot obtain credit for both this course and BIOL-4710.) Prerequisite: BIOL-2120. Spring term annually. 4 credit hours |
| BCBP-4760 Molecular Biochemistry I Part I of a two-semester sequence focusing on the chemistry, structure, and function of biological molecules, macromolecules, and systems. Topics covered include protein and nucleic acid structure, enzymology, mechanisms of catalysis, regulation, lipids and membranes, carbohydrates, bioenergetics, and carbohydrate metabolism. This course is taught in studio mode. (Students cannot obtain credit for both this course and either BIOL-4760 or CHEM-4760.) Prerequisites: CHEM-2250 or CHEM-2210 and BIOL- 2120 or equivalent. Fall term annually. 4 credit hours |
| BCBP-4770 Molecular Biochemistry II The second semester of the molecular biochemistry sequence. Topics include lipids and lipid metabolism, amino acid metabolism and the coenzymes involved in this metabolism, nucleic acid synthesis and chemistry, protein synthesis and degradation, integration of metabolism, photobiology, and photosynthesis. This course is taught in studio mode. (Students cannot obtain credit for both this course and either BIOL-4770 or CHEM-4770.) Prerequisite: BCBP-4760 or equivalent. Spring term annually. 4 credit hours |
| BCBP-4780 Protein Folding The biophysical mechanism of protein folding and the role of misfolding in human diseases is explored. The course will introduce principles of protein structure, protein folding in the cell, and thermodynamic and kinetic methods for studying protein folding in vitro. The course will also involve a literature-based discussion of human diseases related to protein folding defects, including Alzheimer’s and other amyloid diseases, cystic fibrosis, and Prion-related syndromes. Spring term even-numbered years. Prerequisite: BCBP-4760 or equivalent. (Students may not receive credit for both this course and BCBP-6780, CHEM-4780, or CHEM-6780.) 4 credit hours |
| BCBP-4790 Protein Chemistry The ability to design synthetic proteins from first principles (de novo design) is a new area of protein chemistry with exciting potential applications in medicine and industry. This course will review our present understanding of chemistry and physics of protein structure and stability and show how this understanding can be applied to the design of unnatural proteins. The course will also cover the computer modeling and chemical synthesis of proteins, how to impart new characteristics to natural proteins via chemical modification, and the generation of protein ‘chimera’ using semisynthesis. (Students cannot receive credit for this course and BCBP-6790 or CHEM-4790.) Prerequisite: CHEM-4760 or BCBP-4760 or BIOL-4760 or equivalent; CHEM-6190 or BCBP-4810 is an asset. Recommended for seniors; juniors should talk to the instructor before registering. Spring term, odd-numbered years. 4 credit hours |
| BCBP-4810 Biological Spectroscopy Explores the use of spectroscopic methods to study biological systems. Theory and application of techniques including UV-visible absorbance spectroscopy, IR spectroscopy, fluorescence, electron paramagnetic resonance and nuclear magnetic resonance, and their application to the study of the structure of macromolecules, enzyme mechanism, and other important biological problems covered. (Students cannot obtain credit for both this course and BCBP-6810.) Prerequisite: BCBP-4760 or equivalent. Fall term even-numbered years. 4 credit hours |
| BCBP-4860 Protein and Nucleic Acid Structure The three-dimensional structure of these biological macromolecules is explored in detail, with special attention to the relationship of structure and function. Other topics include methods used to determine structure, the thermodynamics of structure formation, structure prediction from primary sequence, and computer-based molecular modeling. (Students cannot obtain credit for both this course and BCBP-6860.) Prerequisite: BCBP-4760 or equivalent. Spring term even-numbered years. 4 credit hours |
| BCBP-4870 Crystallographic Analysis of Protein Structure X-ray crystallography is the method of choice for determining the three-dimensional structure of biological macromolecules. We will cover the crystallographic method, its theory and practice, followed by a detailed exploration of selected protein structures. Other topics include the thermodynamics of structure formation, structure prediction form primary sequence, and molecular dynamics. (Students cannot obtain credit for both this course and BCBP-6870.) Prerequisite: BCBP-4760, MATH-1020, and PHYS-1200 or equivalents. Fall term odd numbered years. 4 credit hours |
| BCBP-6210 Biophysical Methods Topics covered will include electron microscopy of ordered samples, structural databases, hydrodynamics of biological macromolecules, viscosity, sedimentation, translational and rotational diffusion, chromatography, conductance, dielectrophoresis, dynamic light scattering, flow and electric birefringence, and electrophoresis. Also water as a solvent, polyelectyrolytes, and Debye-Huckel theory. (Students cannot obtain credit for both this course and BCBP-4210.) Prerequisite: CSCI-1100, BIOL-2120, CHEM-2440, and PHYS-1100 or equivalents. Spring term odd-numbered years. 4 credit hours |
| BCBP-6310 Genetic Engineering Case studies on the effect of genetic engineering on medicine, agriculture, biology, forensics, and various other areas of technology. Each week a set of assigned readings will be discussed. Some of the topics to be covered are vaccines, biomolecular computing and electronics, paleontology, ecology, bioremediation, and polymers. (Students cannot obtain credit for both this course and BCBP- 4310.) Prerequisite or corequisite: BCBP-4760 and BIOL-4620, or permission of instructor. Fall term, odd-numbered years. 4 credit hours |
| BCBP-6780 Protein Folding The biophysical mechanism of protein folding and the role of misfolding in human diseases is explored. The course will introduce principles of protein structure, protein folding in the cell, and thermodynamic and kinetic methods for studying protein folding in vitro. The course will also involve a literature-based discussion of human diseases related to protein folding defects, including Alzheimer’s and other amyloid diseases, cystic fibrosis, and Prion-related syndromes. (Students may not receive credit for both this course and BCBP-4780, CHEM-4780, or CHEM-6780.) Prerequisite: BCBP-4760 or equivalent. Spring term even-numbered years. 4 credit hours |
| BCBP-6790 Protein Chemistry The ability to design synthetic proteins from first principles (de novo design) is a new area of protein chemistry with exciting potential applications in medicine and industry. This course will review our present understanding of chemistry and physics of protein structure and stability and show how this understanding can be applied to the design of unnatural proteins. The course will also cover the computer modeling and chemical synthesis of proteins, how to impart new characteristics to natural proteins via chemical modification, and the generation of protein ‘chimera’ using semisynthesis. (Students can not receive credit for this course and BCBP-4790 or CHEM-4790.) Prerequisite: CHEM-4760 or BCBP-4760 or BIOL-4760 or equivalent; CHEM-6190 or BCBP-4810 is an asset. Spring term, odd numbered years. 3 credit hours |
| BCBP-6810 Biological Spectroscopy Explores the use of spectroscopic methods to study biological systems. Theory and application of techniques including UV-visible absorbance spectroscopy, IR spectroscopy, fluorescence, electron paramagnetic resonance and nuclear magnetic resonance, and their application to the study of the structure of macromolecules, enzyme mechanism, and other important biological problems covered. (Students cannot obtain credit for both this course and BCBP-4810.) Prerequisite: BCBP-4760 or equivalent. Fall term even-numbered years. 4 credit hours |
| BCBP-6860 Protein and Nucleic Acid Structure The three-dimensional structure of these biological macromolecules is explored in detail, with special attention to the relationship of structure and function. Other topics include methods used to determine structure, the thermodynamics of structure formation, structure prediction from primary sequence, and computer-based molecular modeling. (Students cannot obtain credit for both this course and BCBP-4860.) Prerequisite: BCBP-4760 or equivalent. Spring term even-numbered years. 4 credit hours |
| BCBP-6870 Crystallographic Analysis of Protein Structure X-ray crystallography is the method of choice for determining the three-dimensional structure of biological macromolecules. We will cover the crystallographic method, its theory and practice, followed by a detailed exploration of selected protein structures. Other topics include the thermodynamics of structure formation, structure prediction form primary sequence, and molecular dynamics. (Students cannot obtain credit for both this course and BCBP-4870.) Prerequisite: BCBP-4760, MATH-1020, and PHYS-1200 or equivalents. Fall term odd-numbered years. 4 credit hours |
| BCBP-6940 Readings in Biochemistry/Biophysics Independent study of selected readings in the fields of biochemistry and biophysics, supervised by a faculty member. Prerequisite: permission of instructor. Offered each term. 1 to 4 credit hours |
| BCBP-6990 Master’s Thesis Active participation in research, under the supervision of a faculty adviser, leading to a master’s thesis. Grades of IP are assigned until the thesis has been approved by the faculty adviser and accepted by the Office of Graduate Education to be archived in a standard format in the library. Grades will then be listed as S. 1-9 credit hours |
| BCBP-9990 Dissertation Active participation in research, under the supervision of a faculty adviser, leading to a doctoral dissertation. Grades of IP are assigned until the dissertation has been publicly defended, approved by the doctoral committee, and accepted by the Office of Graduate Education to be archived in a standard format in the library. Grades will then be listed as S. Variable credit hours |
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Rensselaer Polytechnic Institute (RPI), 110 8th St., Troy, NY 12180. (518) 276-6000 Please direct questions regarding this site to catalog@rpi.edu. |