
520(510/610)/Chem. 520. Biophysical Chemistry I.
Chem. 463, Biol. Chem. 415, or Chem 420; permission of course director. (3). (Excl). (BS).
This course is the first of a two term biophysical chemistry series Biophysics 510/511. The course offers an overview of protein, nucleic acid, lipid and carbohydrate structures.
521(511)/Chem. 521. Biophysical Chemistry II.
Chem. 461, Biol. Chem. 415, and Chem. 430; and permission of course director. (3). Excl). (BS).
This course gives background applications of several physical techniques used in biophysical research. General principles of spectroscopy are explained. Macromolecular structure determination by X-ray diffraction and and two-dimensional NMR are treated in detail. IR, Raman, CD, EXAFS, EPR, and ESEEM are introduced.
570/Biol. Chem. 570. Protein Structure.
Introductory biochemistry (Biol. Chem. 415(1). (Excl). (BS).
Detailed description of protein structure and function. Thorough treatment of secondary, super-, secondary, tertiary, and quarternary structure as well as motif and domain patterns. Theoretical and experimental approaches to study protein folding and stability (pathways, thermodynamics) are discussed.
571/Biol. Chem. 570. Nucleotide and Polynucleotide Structure.
Biophysics 570. (1). (Excl). (BS).
Nucleotide, DNA and RNA structure, DNA-protein interaction and fine structure.
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