biochem 001 the structure and function of large biological molecules part 1 (proteins carbohydrates

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mikepl103
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282548
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biochem 001 the structure and function of large biological molecules part 1 (proteins carbohydrates
Updated:
2014-10-02 19:37:45
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biochem 001 biochemistry unity life part proteins carbohydrates lipids nucleic acids
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2014,biology,biochem
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biochem 001 the structure and function of large biological molecules part 1 (proteins, carbohydrates, lipids, nucleic acids) #1
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  1. what is the difference between starch and glycogen?
    starch is linear and glycogen is branched
  2. what are the three types of lipids?
    fats, steroids, and phospholipids
  3. what do we use fats for?
    energy, cushioning, and insulation
  4. two glucose molecules bonded together is called what?
    maltose
  5. a glucose molecule and a fructose molecule bonded together is called what?
    sucrose
  6. what kind of glycosidic linkage is in maltose?
    1,4-glycosidic linkage
  7. what type of glycosidic linkage is found in sucrose?
    1,2-glycosidic linkage
  8. what are proteins used for?
    structural support, storage, transport, cell communication, movement, defense against foreign substances
  9. alanine
  10. aspartic acid
  11. cysteine
  12. what is the primary structure of a peptide?
    the linear sequence of amino acids
  13. what is the secondary structure of a peptide?
    This level of structure describes the local folding pattern of the polypeptide backbone and is stabilized by hydrogen bonds between N-H and C=O groups. Various types of secondary structure have been discovered, but by far the most common are the orderly repeating forms known as the a helix and the b sheet.
  14. what is the tertiary structure of a peptide?
    This level of structure describes how regions of secondary structure fold together – that is, the 3D arrangement of a polypeptide chain, including a helices, b sheets, and any other loops and folds. Tertiary structure results from interactions between side chains, or between side chains and the polypeptide backbone, which are often distant in sequence. Every protein has a particular pattern of folding and these can be quite complex.


    This level of structure involves ionic bonds, disulfide bridges, van der waals forces, hydrogen bonds, and hydrophobic interactions
  15. what is the quaternary structure of a peptide
    when more than one peptide subunit is needed for the protein
  16. where did RNA originate from?
    a parasite
  17. what are the three components of a nucleotide?
    nitrogenous base, sugar, and phosphoryl group
  18. what are the purines?
    adenine and guanine
  19. what are the pyrimidines?
    cytosine, thymine and uracil
  20. by which process are monomers linked to create polymers?
    dehydration reaction

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