| Required Coursework |
Course Descriptions:
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Directors: |
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Physical Biochemistry I
Fall I BSCI 5196-01
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Kim Orth
Credit: 1.5 hours |
Emphasizing quantitative analysis/reading/discussion of the primary literature, course study provides an advanced look at multiple aspects
of biochemistry including protein analysis, mass spectrometry, equilibria, specificity, cooperativity and regulation of macromolecular interactions, sedimentation velocity and equilibrium analysis, and related topics. These principles will be illustrated by the study of well-characterized examples from the iterature.
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Molecular Biophysics: Spectroscopy
Fall II MB 5106-01
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Mischa Machius
Credit: 1.5 hours |
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Covers optical spectroscopy with emphasis on applications in biomedical research. including interaction of light and matter, absorption spectroscopies (UV/vis and infrared), fluorescence, and circular dichroism.
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Quantitative Modeling of Biochemical Signaling Systems I
Spring II MB 5125-0
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Elliott Ross
Credit: 1.5 hours |
| This course explores the quantitative understanding of biological regulatory networks by considering (1) their experimental analysis, (2) their depiction by creation of explicit physical models, (3) reduction of the physical models of mathematical models and (4) the use of the mathematical models to provide mechanistic understanding and drive new and more effective experiments. This course deals mostly with strategy of modeling process and analysis of simple reactions (first- and second-order chemical reactions, diffusion, equilibrium and steady-state systems) and their combination into small signaling modules, with some underlying techniques for working with quantitative data. This course is a pre-requisite for Part II. |
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Modern Methods in Structural Biology
Spring II MB (TBA)
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Kevin Gardner
Credit: 1.5 hours |
Much of modern structural biology is based on results obtained with two high-resolution methods (X-ray crystallography, NMR spectroscopy), often complemented by several lower-resolution approaches (EM, scattering, FRET among others). We assert that the successful union of these general approaches is absolutely critical in modern structural biology, particularly as biophysical methods are applied to larger, multicomponent systems that are often dynamic in their composition. This course provides the foundation for students to understand these techniques, extending the introduction provided in the first year Core Course. A central focus for the course will be discussions of both the theory and application of X-ray crystallography and NMR spectroscopy, with the aim to establish the physical bases of both methods using instruction that covers theory and application. Combined with introductions into the lower-resolution methods, this course will provide students with the ability to critically evaluate the relative strengths and weaknesses of each technique and how they can be effectively combined to provide insight into biological systems.
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| Advanced Program Courses (Electives) |
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Computational Approaches in Protein Science
Spring I MB 5145
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Nick Grishin
Credit: 1.5 hours |
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The basics of computational methods used to analyze protein sequences and structures. Topics include sequence similarity searches using profile-based tools, functional prediction, structure prediction and threading, homology modeling, energy-based simulations, protein classification, and evolutionary concepts: homology inference and tree reconstruction.
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Advanced NMR Spectroscopy
Fall and Spring II MB 5154-01
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Jose Rizo-Rey
Credit: 1.5 hours |
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Principles of nuclear magnetic resonance (NMR), emphasizing its application to macromolecular structure determination. Topics include multidimensional NMR spectroscopy, including COSY, TOCSY and NOESY experiments, sequential assignments and structural analysis, practical methods and new developments in the field. Recommended prerequisites: Modern Methods in Structural Biology.
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Protein Structure and Folding
Fall II MB 5124-01
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Elizabeth Goldsmith
Credit: 1.5 hours |
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Overview of the basic principles governing protein structure and folding. Topics include stereochemical mechanisms by which protein secondary and tertiary structures are generated and stabilized, methods of prediction of tertiary structure from amino acid sequence, and the organization of folding motifs into protein structures. Instruction will be based on didactic material, discussion of the primary literature, and student projects utilizing computer graphics.
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Practical X-Ray Crystollography
Spring I MB 5157-01
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Hong Zhang
Credit: 1.5 hours |
| Practical X-ray Crystallography will mix lectures and hands-on tutorials with the goal of providing beginners in the discipline the tools to move forward confidently on crystallographic projects of their own. In the tutorial section, students will grow protein crystals, collect and process X-ray diffraction data, solve the phase problem using both molecular replacement and anomalous diffraction, build protein models, refine the model, analyze the model, and learn effective model presentation. Students will be tutored in the use of state-of-the-art crystallographic software. In the lectures, the principles behind the methods will be discussed. Modern Methods in Structural Biology is a prerequisite for this course |
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Computational Methods in the Biological Sciences
TBA
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Alexander Pertsemlidis
Credit: 1.5 hours |
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Biocomputing and computational biology are synonyms that describe the use of computers and computational techniques to analyze biological systems, from individual molecules to organisms to higher-order systems. This course will cover the computational techniques used to access, analyze, and interpret the biological information in common types of biological databases and the biological questions that can be addressed by such methods, applicable to the study of the context of genes within the same genome and across different genomes, the study of molecular sequence data for the purpose of inferring the function, interactions, evolution, and structure of biological molecules, and the study of annotation and ontology.
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Quantitative Analysis of Genes and Genomes
Fall -BSCI-TBA
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Alexander Pertsemlidis
Credit: 1.5 hours |
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Advances in biotechnology are making it possible to obtain massive amounts of data about the genetic information contained in living cells, the transmission of this information from parent to child, the changes in the information over evolutionary time, and the manner in which this information influences the chemical activity of cells. This course is an introduction to algorithmic techniques for the acquisition, analysis and interpretation of such data.
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| Recommended Courses in Other Programs |
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Physical Biochemistry II
Fall II TBA
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Meg Phillips
Credit: 1.5 hours |
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Provides students with a basic understanding of enzyme mechanism and enzyme kinetic analysis. Topics to be covered include basic Michaelis-Menten kinetics, multisubstrate reactions and inhibitor studies ranging from the methods to analyze simple competitive inhibitors to suicide or tight binding inhibitors. These principles will be illustrated for a series of classic well-characterized enzyme reactions. Emphasis is placed on quantitative analysis through a series of problem sets and through reading and discussion of the primary literature.
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Structure and Function of Ion Channels
Fall I NS5164-01
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Ilya Bezprozvanny
Credit: 1.5 hours |
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The operation of the nervous and muscular systems rests upon the activities of a constellation ion channels, which mediate electrical signaling by action potentials, intracellular communication by electrical and chemical synaptic transmission, transduction of sensory stimuli, and the excitation-contraction coupling. Drawing upon the techniques of biophysics, biochemistry, and molecular biology, students in this course will consider the structures and functions of representative channels.
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Bioinformatics and DNA Microarray Data Analysis
Fall IMM5101-01
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Thomas Scheuermann
Credit: 1.5 hours |
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High-throughput methodologies are generating complex experimental data at an incredible rate. As a result, these developments are forcing a paradigm shift in how the result from biological experimentation are interpreted, in which computers are playing an increasingly important role. The increasing use of computers for data storage, data retrieval, and data analysis is leading to the evolution of two biological disciplines - bioinformatics and computational biology. In this course, we will use the gene expression microarray experimental platform as a model highthroughput methodology to examine how bioinformatics, statistics and computation are being used to support the discovery of new biomedical knowledge. In addition to didactic lectures and discussion, this class will include a series of hands-on workshops focused on the basic steps for microarray data processing.
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