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BIOLOGY 1210 > Proteins > Flashcards

Proteins Flashcards

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1
Q

what is the monomer of proteins?

A

amino acids

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2
Q

what is the polymer of amino acids? what re they made from?

A

polypeptide

- constructed from same set of 20 amino acids

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3
Q

what is the structure of protein?

A

one or more polypeptides folded into specific 3-D structure

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4
Q

how many different amino acids are there?

A

20

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5
Q

what are some functions of proteins?

A
  • speed up chemical reactions
  • provide structural support
  • provide transport
  • are hormones
  • allow for movement
  • defend our bodies against foreign invaders
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6
Q

what do all amino acids have in common?

A

-have the same common structure, with differing R-groups

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7
Q

what do r-groups determine?

A

Chemical properties of the R-groups determines the unique characteristics of an amino acid

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8
Q

what are the components of an amino acid?

A
  • amino group (N1 H2)
  • central carbon (with a hydrogen atom attached)
  • carboxyl group (C with double bonded O and single bonded hydroxyl)
  • varying r-groups
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9
Q

which amino acids are hyrdophobic? hydrophilic?

A

Hydrophobic –> Nonpolar amino acids

Hydrophilic –> Polar amino acids; and charged amino acids

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10
Q

how are 2 amino acids linked? what kind of bond do they form? what is this kind of bond between 2 amino acids called?

A

by removal of water molecule

  • covalent
  • peptide bond
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11
Q

what does the backbone of a polypeptide consist of?

A

-amino group, carboxyl group, central carbon and hydrogen

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12
Q

where does the peptide bond form between amino acids?

A

between the hydroxyl (of the carboxyl) and an hydrogen of the amino group –> to form water molecule (tehrefor removing H and OH

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13
Q

how are functional proteins formed?

A

one or more polypeptides must fold into a specific shape

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14
Q

What determines a protein’s unique shape?

A

The amino acid sequence

-Shape determined and maintained by interactions between the different amino acids

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15
Q

what does a proteins structure determine? how many levels of structure do proteins have? what are they?

A

it’s function

  • proteins have 4 levels of structure
    1. primary
    2. secondary
    3. tertiary
    4. quaternary
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16
Q

in the backbone of polypeptide what kind of bond is formed between the C, O, and N? what does this result?

A
  • polar covalent bonds
  • results in atoms that are unfairly sharing electrons, therefore they have partial charges –> with partial charges they can form hydrogen bonds
17
Q

Primary protein structure:

  1. what is the shape
  2. how is it held together
  3. what kind of proteins do you find this in?
  4. how many polypeptides are involved
A
  1. linear sequence of amino acids
  2. held together by peptide bonds (covalent bonds between monomers)
  3. all proteins have this level of structure
  4. one polypeptide
18
Q

Secondary protein structure:

  1. what is the shape/structures
  2. how is it held together
  3. what are the 2 types of secondary structures?
  4. how many polypeptides are involved
A
  1. coiled and/or folded into particular shapes - local folded structures that form within a polypeptide
  2. hydrogen bonds forming between between atoms in polypeptide backbone (not r-groups)
  3. Alpha-helix and beta-pleated
  4. one polypeptide
19
Q

what is an alpha helix?

A

a coil held together by hydrogen bonds between backbones of amino acids (is made of only one polypeptide)

20
Q

what are beta-pleated sheets?

A

two or more regions within a single polypeptide lying side by side, connected by hydrogen bonds between parts of the two parallel polypeptide backbones

21
Q

Tertiary protein structure:

  1. what is the shape
  2. how is it held together
  3. how many polypeptides are involved
A
  1. overall rounded or globule shape
  2. held together by interactions between r-groups within single polypeptide. can have many different types of interactions occurring at once
  3. single polypeptide which is all folded up
22
Q

what are 4 types of interactions that may be occurring between r-groups and which kinds of amino acids are involved?

A
  1. hydrophobic interactions –> non-polar amino acids
  2. hydrogen bonds –> polar amino acids
  3. ionic bonds –> charged amino acids
  4. covalent bonds (disulfide bridges) –> between sulfhydryl groups
23
Q

Quaternary protein structure:

  1. how is it held together
  2. what kind of proteins do you find this in?
  3. how many polypeptides are involved
A
  1. held together by interactions between r-groups of different polypeptides
  2. Only proteins made up of multiple sub units have this level of structure
  3. 2 or more polypeptide chains interacting with one another
24
Q

what are fibrous proteins? what is often their function? give an example

A
  • polypeptide chains that are arranged in long strands or sheets
  • often for structural purposes
  • eg. collagen - has primary, secondary and quaternary levels of structure
25
Q

what are globular proteins? what is often their function? give an example

A

-polypeptide chains that folded into spherical shapes
-often are enzymes, transport proteins, receptor proteins, or hormones
-eg. hemoglobin - has primary, tertiary, and quaternary
levels of structure

26
Q

what are 3 factors that affect a proteins structure? changes in these conditions may cause what?

A
  1. Temperature
  2. pH
  3. Salt concentration
    - may cause a protein to denature (destroy the characteristic properties of) and lose its function
27
Q

how is protein structure affected by temperature? which levels of structure are effected by increase in temp, why? which level of structure is relatively unaffected, why?

A
  • temp causes an increase/decrease of movement of particles.
  • Heat increases the kinetic energy and causes the molecules to vibrate so rapidly and violently that hydrogen and hydrophobic bonds are disrupted
  • cold decreases the kinetic energy and once cold enough, causes proteins to become solid and stop their functions
  • levels 2, 3, and 4 –> because held together with hydrogen and hydrophobic interactions (which are weak)
  • level 1 –> because held together with covalent bonds which are strong
28
Q

how is protein structure affected by change in pH? which kinds of bonds will changes in pH affect?

A
  • when there is an increase/decrease in the amount of pH, it changes how many hydrogen ions there are in the environment
  • Increase in H+ → decrease in OH-
  • Increase in OH- –> decrease H+
  • Will disrupt ionic and hydrogen bonds, and hydrophobic interactions
29
Q

which levels of structure will be effected by change in pH, why? which level of structure will remain relatively unaffected, why?

A
  • level 2 –> because held together with hydrogen bonds

- level 3 and 4 –> because held together with mix of hydrogen, ionic, and hydrophobic bonds/interactions

30
Q

how is protein structure effected by change in salt concentration? which kinds of bonds will changes salt concentration affect?

A
  • when there is an increase/decrease in the salt concentration, it changes how many hydrogen ions there are in the environment
  • Will disrupt ionic and hydrogen bonds, and hydrophobic interactions
31
Q

which levels of structure will be effected by change in salt concentration, why? which level of structure will remain relatively unaffected, why?

A
  • level 2 –> because held together with hydrogen bonds

- level 3 and 4 –> because held together with mix of hydrogen, ionic, and hydrophobic bonds/interactions

BIOLOGY 1210 (26 decks)

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