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Course Criteria
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4.00 Credits
X-ray crystallography and nuclear magnetic resonance (NMR) are used to determine 3-D structures of biological macromolecules at atomic resolution. The course will cover crystallographic and NMR methods, their theory and practice, along with thermodynamics of structure formation and molecular dynamics. Students will prepare a poster presentation on a protein of their choice. (Students cannot obtain credit for both this course and BCBP 6870.) Prerequisites/Corequisites: Prerequisites: BCBP 4760, MATH 1020, and PHYS 1200 or equivalents. When Offered: Fall term even numbered years. Credit Hours: 4
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4.00 Credits
Independent laboratory research, on or off campus, supervised by a faculty member, culminating in a written thesis; or literature research culminating in the writing of a review article. The thesis research must also be presented in the form of a poster presentation or a talk. This is a communication-intensive course. Prerequisites/Corequisites: Prerequisite: permission of instructor. When Offered: Offered each term. Credit Hours: 4
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4.00 Credits
Advanced graduate course covering fundamental aspects of NMR common for application in a broad range of fields. Classical and quantum-mechanical descriptions are utilized to explore information content of NMR pulse sequences. The latter approach includes density matrix theory and proceeds with the product-operator formalism. Practical aspects and data analysis are also described. Subsequent focus is on liquid-state NMR of biological macromolecules, including resonance assignment and determination of molecular structure and dynamics. (Students cannot obtain credit for both this course and CHEM 6170.) Prerequisites/Corequisites: Prerequisite: CHEM 4410 or equivalent. When Offered: Spring term annually. Credit Hours: 4
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4.00 Credits
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.) Prerequisites/Corequisites: Prerequisites or corequisites: BCBP 4760 and BIOL 4620, or permission of instructor. When Offered: Fall term, odd-numbered years. Credit Hours: 4
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3.00 Credits
Characterization of patterns and changes in patterns of protein expression with development, aging, and disease. Protein separation and quantification strategies; mass spectrometry and analysis of spectra; protein profiling, biomarkers, post-translational modifications; current applications; emerging technologies and applications. Individual presentations on relevant topics will be expected. (Students cannot obtain credit for this course and BCBP 4640, BIOL 4640 or BIOL 6640.) Prerequisites/Corequisites: Prerequisite: BCBP 4760 or equivalent. When Offered: Spring term annually. Credit Hours: 3
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4.00 Credits
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.) Prerequisites/Corequisites: Prerequisite: BCBP 4760 or equivalent. When Offered: Spring term even-numbered years. Credit Hours: 4
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4.00 Credits
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.) Prerequisites/Corequisites: Prerequisite: BCBP 4760 or equivalent. When Offered: Fall term even-numbered years. Credit Hours: 4
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4.00 Credits
X-ray crystallography and nuclear magnetic resonance (NMR) are used to determine 3-D structures of biological macromolecules at atomic resolution. The course will cover crystallographic and NMR methods, their theory and practice, along with thermodynamics of structure formation and molecular dynamics. Students will prepare an oral presentation on a protein of their choice. (Students cannot obtain credit for both this course and BCBP 4870.) Prerequisites/Corequisites: Prerequisites: BCBP 4760, MATH 1020, and PHYS 1200 or equivalents. When Offered: Fall term even-numbered years. Credit Hours: 4
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1.00 - 4.00 Credits
Independent study of selected readings in the fields of biochemistry and biophysics, supervised by a faculty member. Prerequisites/Corequisites: Prerequisite: permission of instructor. When Offered: Offered each term. Credit Hours: 1 to 4
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3.00 Credits
Active participation in a semester-long project, under the supervision of a faculty adviser. A Professional Project often serves as a culminating experience for a Professional Master's program but, with departmental or school approval, can be used to fulfill other program requirements. With approval, students may register for more than one Professional Project. Professional Projects must result in documentation established by each department or school, but are not submitted to the Graduate School and are not archived in the library. Grades of A, B, C, or F are assigned by the faculty adviser at the end of the semester. If not completed on time, a formal Incomplete grade may be assigned by the faculty adviser, listing the work remaining to be completed and the time limit for completing this work.
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