2009-09-18_-_Lecture_7

2009-09-18_-_Lecture_7 - Biochemistry 461 FS 2009 Michigan...

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Biochemistry 461 FS 2009 Michigan State University Proteins: Structure and Folding September 18, 2009 Lecture 7 • A handful of architectures dominate sequenced genomes. •N in e folds are observed again and again, accounting for 40% of the domain structures in the protein data bank (i.e., available 3D structures). Annual Review of Biochemistry 74 , 867-900, 2005. Relatively Few Different Folds (from previous lecture) • Protein tertiary structure is more reliably conserved than primary structure • Protein structure can provide information about evolution • Proteins with high sequence similarity, structure, and function are in the same
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Serum albumin (all- α) CD8 (all- β) Protein Families (from previous lecture) Alcohol dehydrogenase ( α/β) Thymidylate synthase ( α + β) 3 Quaternary structure is the association of multiple polypeptide chains ( subunits ) into a single protein structure. • Vary from small complexes to huge assemblies • Subunits can be the same, very similar or completely different. • Often have some form of symmetry Hemoglobin Quaternary Structure (from previous lecture) 4
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1.) X-ray crystallography • Crystallization into a regular lattice (sometimes very hard!); • typically the bottleneck • Measurement of an x-ray diffraction pattern ; • Calculation of an electron density ; • Fitting of the protein covalent structure to the electron density; • Refinement to the final three-dimensional structure. Determining the 3-D Structure of a Protein 5 • NMR has disadvantages in efficiency, precision, and maximum size • But, NMR is a solution technique (does not require a single crystal), and can yield additional information about flexibility/dynamics, ligand binding, and other parameters. Determining the 3-D Structure of a Protein
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This note was uploaded on 01/17/2012 for the course NSC 461 taught by Professor Benning during the Fall '11 term at Michigan State University.

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2009-09-18_-_Lecture_7 - Biochemistry 461 FS 2009 Michigan...

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