AP Bio Units 1.4-1.7

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33 Terms

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Carbohydrates CHO ratio

1:2:1

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Carbohydrates structure

monosaccharides → poly saccharides

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simple sugars function

quick energy

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complex carbs function

long term E storage or structure

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lipid structure

CHO (mostly CH)

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CH is …

nonpolar & hydrophobic

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saturated fatty acids have

only single bonds

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unsaturated fatty acids have

at least 1 2x bond → chain kinks

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(lipids) more 2x bonds →

more liquid @ room temp (more unsaturated)

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Phospholipids

  • nonpolar fatty acid tails form membrane interior

  • away from aqueous intracellular & extracellular environment

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fats function

  • E storage

  • insulation for mamals

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steroids function

hormones

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cholesterol function

structural stability in cell membranes of animals

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phospholipids function

lipid bilayer of membranes

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Nucleic Acids structure

  • CHO + N & P

  • made of

    • 5 carbon sugar

    • a phosphate

    • a nitrogenous base

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what do dna & rna do

encode info

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nitrogenous bases

all organisms follow same pairing rules

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Purines

Double rings (AG)

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Pyrimidines

single rings (CUT)

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Pyrimidines pair w/

purines

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Nucleic acids directionality

NA sequences have ends based on 3’ hydroxyl & 5’ phosphate of the sugar

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during nucleic acid synthesis nucleotides can only be added to

the 3’ end of the growing strand

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DNA structure

  • antiparallel 2x helix

  • 2 strands of nucleotides running in op directions

  • 5’ to 3’ orientation

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DNA

  • deoxyribose

  • ATCG

  • double stranded

  • contains genes to code for proteins

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RNA

  • ribose

  • AUCG

  • single stranded

  • involved in protein synthesis

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protein structure

chains of amino acids connected by peptide bonds

  • polypeptides

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Amino acids

  • made of central carbon, amine grp, carboxyl grp, & R grp

  • 20 diff AAs

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AA r groups can be

  • polar

  • nonpolar

  • ionic

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r group interactions …

determine the structure & function of each part of a protein

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primary level of protein structure

sequence of AAs in a protein

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secondary levl of protein structure

forms due to H bonds btwn backbones of neighboring AAs

  • alpha-helices

  • beta-pleated sheets

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tertiary level of protein structure

  • 3D shape

  • results from r group interactions

    • H bonds

    • hydrophobic interactions

    • ionic interactions

    • disulfide bridges (cov. bonds)

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quaternary lvl of protein structure

Interactions btwn multiple polypeptides to produce a functional protein

NOT APPLICABLE TO ALL PROTEINS