Biological Molecules part 2

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  1. When acid dissolves in water, they release __
    hydrogen ions: H+ (protons)
  2. Bases __ H+ ions
    accepts

    (H+ ions can attach to other molecules & change their properties)
  3. pH is the measure of __
    hydrogen ion concentration (H+)
  4. The pH scale indicates __
    the strength of a solution of an acid or base

    (A pH of 7 means the concentration of H+ ions is 1 x 10^-7 of water)

    (page 41 on slide)
  5. 4 major types of biological molecules
    • proteins
    • carbohydrates
    • lipids
    • nucleic acids

    (All are polymers except lipids)
  6. Proteins are combinations of __
    20 amino acids
  7. Carbs are __ linked to form __
    sugar monomers (monosaccharides); polysaccharides
  8. Nucleic acids are made up of __
    4 kinds of nucleotide monomers

    i.e. DNA & RNA
  9. Lipids: __ forces maintain interactions between __
    Noncovalent; lipid monomers

    (phospholipid makes up cell membrane)
  10. Out of the types of macromolecules, our body contains mostly __
    protein (polypeptides)

    (page 44 on slide)
  11. Condensation (Dehydration Synthesis)
    2 monomers produce a polymer (forms bonds)

    (page 45 on slide)
  12. Hydrolysis
    Polymer splits into monomers

    (page 46 on slide)
  13. types of proteins (functions)
    • enzymes: accelerate (catalyze) reactions
    • defensive proteins (antibodies)
    • hormonal & regulatory proteins
    • receptor proteins: monitor cellular activity
    • storage, structure, transport
    • genetic regulatory proteins
  14. __ are NOT done by proteins
    energy & information storage
  15. __ determines the structure of proteins
    The primary amino acid sequence
  16. The amino acid structure is made up of __
    • carbon
    • hydrogen
    • amino group (H3N+)
    • carboxyl group (COO-)
    • side chain (R)

    (page 48 on slide)
  17. Amino acids with polar side chains are __
    hydrophilic (charged & uncharged)

    (page 49 & 50 on slide)
  18. Amino acids with nonpolar uncharged side chains are __
    hydrophobic

    (page 51 on slide)
  19. amino acid special cases
    • Cysteine (Cys)
    • Glycine (Gly)
    • Proline (Pro)

    (page 52 on slide)
  20. Cysteine
    forms disulfide bonds which affects the 3D structure of the protein

    sideĀ chain: CH2-SH

    (page 53 on slide)
  21. Glycine
    • small, fits in tight corners
    • serves as a neurotransmitter

    side chain: H

    (page 54 on slide)
  22. Proline
    found at bends & loops

    side chain (connects to carbon & amino group): CH2-CH2-CH2

    (page 55 on slide)
  23. Amino acids bond together covalently in a __ reaction by __ linkages/bonds
    condensation (dehydration synthesis); peptide

    (page 56 on slide)
  24. The first amino acid in a polypeptide is the __ terminus, whereas the last amino acid in a polypeptide is the __ terminus
    N; C

    (page 57 on slide)
  25. The primary protein structure is determined by __ bonds and and the secondary structure is determined by __ bonds
    peptide; hydrogen (H)
  26. primary level of protein structure
    the sequence of amino acids in a polypeptide

    (page 59 on slide)
  27. secondary levelĀ of protein structure: alpha helix
    H-Bonds form between the hydrogen of one amino acid & oxygen of another amino acid

    (page 60 on slide)
  28. secondary level of protein structure: beta pleated sheet
    H-bonds form between hydrogen & oxygen, but in a side-by-side arrangement.

    (This can be the same polypeptide folded back on itself, or 2 different polypeptides.)

    (page 61 on slide)
  29. tertiary level of protein structure
    Bending & folding results in a macromolecule with specific 3D shape.

    The outer surfaces present functional groups that can interact with other molecules.

    (page 63 on slide)
  30. Tertiary structure (of protein) is determined by interactions of __
    R-groups:

    • disulfide bridges
    • hydrogen bonds
    • aggregation of hydrophobic side chains
    • van der Waal forces
    • ionic bonds
  31. quaternary level of protein structure
    results from the interaction of subunits of hydrophobic interactions, van der Waal forces, ionic bonds, & hydrogen bonds

    Each subunit has its own unique tertiary structure

    example: hemoglobin

    (page 66 on slide)

Card Set Information

Author:
sophathida
ID:
323461
Filename:
Biological Molecules part 2
Updated:
2016-09-24 01:09:36
Tags:
biology ph macromolecules protein
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Description:
Week 1: Ch. 2, 3
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