Lecture6 - BCH 227 FALL 2010 LECTURE 6: 3-D STRUCTURE OF...

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1 The Three-Dimensional Structure of Proteins BIOCHEM 227 FALL 2010 Lecture 6 Friday, September 10, 2010 TODAY • Continued: structure determination • Protein secondary structure • Protein tertiary structure • Protein quarternary structure • Membrane protein structure BCH 227 FALL 2010 LECTURE 6: 3-D STRUCTURE OF PROTEINS 10 SEP 2010
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2 NMR Spectroscopy • Fundamental concept: – The nuclear magnetic resonance state of a proton is affected by nearby protons – The NMR signals they emit encode distance information – If we know all the interproton distances, we can calculate the structure NMR Spectra (GrsA epimerase, by Cheng-Yu Chen) BCH 227 FALL 2010 LECTURE 6: 3-D STRUCTURE OF PROTEINS 10 SEP 2010
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3 NMR Structures (Ssu72, by J. Werner-Allen) Cryo-EM • Fundamental concept: – Electron microscopes can directly see very small (sub-microscopic) objects – Cooling reduces radiation damage, allows proteins to be protected in ice, lowers thermal motion BCH 227 FALL 2010 LECTURE 6: 3-D STRUCTURE OF PROTEINS 10 SEP 2010
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4 Cryo-EM (Nogales Lab, Berkeley) Studying Protein Function • Detecting interactions between molecules • Measuring enzymatic activity • Examining dynamic behavior Also: genetic methods, etc. BCH 227 FALL 2010 LECTURE 6: 3-D STRUCTURE OF PROTEINS 10 SEP 2010
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5 Protein Secondary Structure Proteins • Long chains of amino acids –wh ich often fold into complex conformations BCH 227 FALL 2010 LECTURE 6:
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6 Some Principles • Proteins are stabilized by having a hydrophobic core and charges on the outside Some Principles • Hydrogen bonds play an extremely important role in protein structure BCH 227 FALL 2010 LECTURE 6: 3-D STRUCTURE OF PROTEINS 10 SEP 2010
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Lecture6 - BCH 227 FALL 2010 LECTURE 6: 3-D STRUCTURE OF...

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