BIOC12H3 Lecture Notes - Lecture 5: Electron Transport Chain, Hp 30B, Bacteriorhodopsin
21 Jul 2013
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Document Summary
Useful in protein analysis -> can be used in fluids, not crystals. Within a magnetic field, proteins absorb electromagnetic radiation differently. Absorbance primarily influenced by neighbor atoms -> allows study of atoms close together. Must be combined with amino acid sequence proteins. Useful only for small proteins -> x-rays are a lot faster. Nmr allows the viewing of disulfide bridges, which are absent in crystal structure. Rnase a: very small and stable protein, first used to understand naturation and denaturation, often times, thought to be too stable! When comparing the structure of ribonuclease between bovine and humans: the structures are very similar! Thus, have very similar active sites: very slight differences (note the location of the beta sheets. Peptide bonds are between carbonyl oxygen + amide hydrogen, on adjacent alpha carbons. Rigid planar structure gives resonance: 40% double bond character! Peptide bonds can be shown as both single or double bonds. Double bond nature of the c-n caused by resonance!
