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lecture outlines for posting6

lecture outlines for posting6 - Lecture 6 EEB 13 24 January...

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Lecture 6 – EEB 13 – 24 January 2008 Dr. Hespenheide [genetic material is DNA, base pairs of DNA molecules code for proteins] proteins - mostly enzymes, facilitate chemical reactions macromolecules, chains (polymers) of amino acids AA 1 AA 2 AA 3 AA 4 AA 5 AA 6 .... AA n - length of proteins - 10’s 100’s of AA’s amino acids - structure H H H HN - C - COOH vs. H - C - COOH R H [amine] [acid] [acetic acid - vinegar] - amino acids combined by condensation - H removed from the amine group and an OH from the acid group to make the H 2 O, water - kinds -20 different amino acids in proteins of living organisms - different “R’s” - [many other kinds of amino acids known than those in proteins] genetic code DNA protein sequence of sequence of base pairs amino acids [DNA] BP - BP - BP - BP - BP - BP - etc ....... A - T - C - G - A - T - etc ....... [protein] AA 1 AA 2 AA 3 etc . - thus a “triplet code” - 3 base pairs 1 amino acid (DNA) (protein) - “sequencing the human genome” = determining the sequence of the base pairs of DNA of all 23 different chromosomes - every individual has slightly different DNA, so we can identify relationships among individuals, identify criminals, et .
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structure of proteins determines activity as enzymes - 4 levels of structure primary structure - sequence of AA’s, not functional by itself - “sequencing proteins” = determining primary structure [secondary structure - not important] tertiary structure - pattern of “folding” of molecule - folding forms “active sites” - places where reacting compounds bind - unfolded protein said to be “denatured,” not functional; e.g. , heating (cooking) denatures proteins (of food) quaternary structure - several “polypeptides” form protein - example: hemoglobin - carries O 2 in blood composed of 4 polypeptides: 2 α chains + 2 β
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