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Department of
Chemistry & Biochemistry

103 Chemistry and Biochemistry Building
PO Box 173400
Bozeman, MT 59717
Tel: 406-994-4801
Fax: 406-994-5407

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Department of Chemistry and Biochemistry

Graduate Course Options


Biochemistry Courses
BCHM 524 - Biochemical Applications of Mass Spectrometry
BCHM 526 - Advance Protein Nuclear Magnetic Resonance Spectroscopy
BCHM 543 - Proteins
BCHM 544 - Molecular Biology
BCHM 545 - Advanced Physical Biochemistry
BCHM 550 - Principles of Structure Determination by X-Ray Crystallography
BCHM 580 - Special Topics in Biochemistry
MEDS 514 - MOLECULAR & CELLULAR BIOLOGY
Chemistry Courses
CHEM 515 - Structure and Bonding in Inorganic Chemistry
CHEM 516 - Mechanics and Dynamics in Inorganic Chcmistry
CHEM 523 - Organic Reaction Mechanisms
CHEM 533 - Physical Organic Chemistry
CHEM 535 - Reagent Chemistry
CHEM 540 - Organic Synthesis
CHEM 551 - Organic Structure Elucidation
CHEM 554 - Organometallic Chemistry
CHEM 557 - Quantum Mechanics
CHEM 558 - Classical and Statistical Thermodynamics
CHEM 559 - Kinetics and Dynamics
CHEM 564 - Advanced Quantum Chemistry
CHEM 580 - Biomaterials Chemistry

Course Descriptions - Biochemistry


BCHM 524 Biochemical Applications of Mass Spectrometry
Instructor: Brian Bothner
Credits: 3
Mass spectrometric can be ued to analyze almost any biolmolecule. This course covers the wide range of methods for ionization, mass analyzers, and data analysis. Upon completion, students will be able to interpret mass spec data and design experiments for their research.
Prerequisite(s): instructor approval

BCHM 526 Advance Protein Nuclear Magnetic Resonance Spectroscopy
Instructor: Valérie Copié
Credits: 3
The course is designed for students to acquire the tools and skills necessary to establish an in-depth understanding of multidimensional (1D, 2D, 3D, 4D) multinuclear (1H, 13C, 15N, 2H) nuclear magnetic resonance experiments that are used in the modern field of NMR-based structural biology. This knowledge will include learning how to analyze nuclear spin evolutions in terms of classical vector models, spin density matrices, and product operator formalism. Students will learn to analyze pulse sequence schemes for magnetization transfer, selective excitation, water suppression, proton and heteronuclear spin decoupling, and other commonly used pulse sequence modules. The students will learn how to utilize nuclear spin parameters for protein structure determination including protocols for resonance assignments, structural calculations using simulated annealing protocols, and interpretation of NMR relaxation parameters (15N-T1, 15N-T2, {1H}-15N-nOe) in terms of internal motions of protein atoms.
Course Web Site: http://chemistry.montana.edu/~copie/teaching.html

BCHM 543 Proteins
Instructor: Valérie Copié
The course is based on lecture, discussion, and reading of current literature scientific topics pertaining to the field of protein research. The course involves extensive reading assignments in both the textbook and scientific journal articles selected by the instructor i.e. research papers, review articles from Science, Cell, Biochemistry, Journal of Biological chemistry etc. Students are paired and expected to make a 20-30 minute presentation and lead discussion of assigned papers. All students are expected to attend each class session and to participate in in-depth paper discussions. As noted on page 4 regarding grading, class participation, student reading and writing, as well as student presentation will count for than 50% of the student grade. The course is intended to provide in-depth exposure to current research topics in the field of Biochemistry. Students learn to critically read and evaluate current scientific literature, experimental data presented in scientific journals, and how to synthesize their own scientific ideas and hypotheses from fundamental knowledge acquired through textbook and reading of scientific papers. Students are also exposed to various aspect of protein chemistry from biophysical characteristics of proteins (non-covalent interactions stabilizing protein structures, thermodynamics properties of proteins, protein folding, post-translational modifications, protein processing, and protein evolution), to more specialized topics such as protein degradation, molecular chaperones, transcription factors, signal transduction machinery etc.).
Prerequisite(s): undergraduate protein course
Course Web Site: http://chemistry.montana.edu/~copie/teaching.html

BCHM 544 Molecular Biology
Instructor: Valérie Copié
Credits: 3
Recent advances in understanding and research methods using both eukaryotic and prokaryotic systems.
Prerequisite(s): BCHM 441, BIOL 302, MB 449 or comparable course

BCHM 545 Advanced Physical Biochemistry
Instructors: Brian Bothner, Martin Lawrence
Credits: 3
Theoretical presentation of the molecular structures and interactions occurring in proteins and nucleic acids. Discussion of spectroscopy techniques used to study bio-molecular structures and function. Includes concepts in: Nuclear Magnetic Resonance, X-ray Diffraction, Ultraviolet Absorption, Fluorescence, Circular Dichroism, Vibrational Spectroscopy and molecular motion, sedimentation and viscosity.
Prerequisite(s): CHEM 324 and BCHM 441

BCHM 550 Principles of Structure Determination by X-Ray Crystallography
Instructor: Martin Lawrence
Credits: 3
This course focuses on theory and practice of molecular structure determined by x-ray crystallography. Topics include crystallography of macromolecules, molecular structure determination from x-ray data, and evaluation of the quality of the resulting macromolecular methods.
Prerequisite(s): BCHM 441 and BCHM 442 or comparable course and Math 182

BCHM 580 Special Topics in Biochemistry
Instructor: Trevor Douglas

Course Web Site: http://www.chemistry.montana.edu/bchm580

MEDS 514 MOLECULAR & CELLULAR BIOLOGY
Instructor: Martin Teintze
Credits: 5
The course covers the medically relevant aspects of biochemistry at an advanced undergraduate level. Topics include protein structure/function, nucleic acids and molecular biology, signal transduction, bioenergetics and carbohydrate metabolism, lipid metabolism and nitrogen metabolism. Clinical correlations will be stressed. T
Course Web Site: http://chemistry.montana.edu/WWAMI/

Course Descriptions - Chemistry


CHEM 515 Structure and Bonding in Inorganic Chemistry
Instructor: Robert Szilagyi
Credits: 3
The primary objective of this course is to define the basic concepts of structure and bonding in coordination compounds, including atomic theories, valence bond and molecular orbital theories, and to demonstrate the use of these theories in problems of inorganic and organometallic chemistry. A secondary objective is to provide basic knowledge for interpreting spectroscopic features and describing trends employing theoretical models.
Course Web Site: http://chemistry.montana.edu/~szilagyi/teaching.html

CHEM 516 Mechanics and Dynamics in Inorganic Chcmistry
Instructor: Edwin Abbott
Credits: 3
Mechanisms and dynamics of the reactions of coordination and organometallic compounds
Prerequisite(s): Chemistry 334 or other undergraduate upperclass inorganic course

CHEM 523 Organic Reaction Mechanisms
Instructor: Cynthia McClure
Credits: 3
A problem solving course concentrating on analyzing organic reactions and transaformations via electron-pushing mechnisms. Problems chosen will be from the current chemical literature. Designed for incoming graduate students and upper-class undergraduates who want to learn or brush up on their electron-pushing skills
Prerequisite(s): Completion of one year of Organic Chemistry

CHEM 533 Physical Organic Chemistry
Instructor: Mary Cloninger
Credits: 3
A semi-quantitative description of the mechanisms of organic reactions. Topics include molecular orbital theory, orbital symmetry, addition and elimination reacions, the kinetics and thermodynames of organic reactions, solvent effects, etc.
Prerequisite(s): Chemistry 417 or comparable course
Course Web Site: http://www.chemistry.montana.edu/chem533

CHEM 535 Reagent Chemistry
Instructor: Trevor Rainey
Credits: 3
A thorough study of synthetic processes, methodologies and reagents
Prerequisite(s): Chemistry 417 or comparable course

CHEM 540 Organic Synthesis
Instructor: Paul Grieco
Credits: 3
A thorough study of strategies for the synthesis of complex natural products
Prerequisite(s): Chem 533 and CHEM 535

CHEM 551 Organic Structure Elucidation
Instructor: Cynthia McClure
Credits: 3
Spectroscopic structure elucidation of small organic molecules. Techniques to be discussed include 1-D and 2-D NMR spectroscopy, UV, IR and Raman spectroscopies. Emphasis will be on interpreting spectra to deduce the structure of the compound in question.
Prerequisite(s): Chem 417 or comparable course

CHEM 554 Organometallic Chemistry
Instructor: Thomas Livinghouse
Credits: 3
Application of organometallic chemistry to organic transformation.
Prerequisite(s): Chem 334 and CHEM 417 or comparable courses

CHEM 557 Quantum Mechanics
Instructor:
Credits: 3
Applications of quantum mechanics to molecules and spin systems
Prerequisite(s): undergraduate Physical Chemistry

CHEM 558 Classical and Statistical Thermodynamics
Instructor:
Credits: 3
Classical and statistical thermodynamics applied to chemical systems
Prerequisite(s): undergraduate Physical Chemistry

CHEM 559 Kinetics and Dynamics
Instructor: Timothy Minton
Credits: 3
Chemical kinetics, theories of reaction rates, molecular reaction dymanics, with applications to chemical reactions in the gas phase, on surfaces and in solution.
Prerequisite(s): undergraduate Physical Chemistry

CHEM 564 Advanced Quantum Chemistry
Instructor: Patrik Callis
Credits: 3
Time independent and time dependent quantum mechanics with application to chemical bonding and molecular spectroscopy
Prerequisite(s): CHEM 557 or equivalent

CHEM 580 Biomaterials Chemistry
Instructor: Trevor Douglas

Course Web Site: http://www.chemistry.montana.edu/chem580



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