Chapter 16 Amino acids, proteins, Flashcards

1
Q

what is hemoglobin and myoglobin an example of?

A

proteins that transport oxygen in the blood

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2
Q

what is found in an amino acid?

A

central atom bonded to an ammonium group(NH3+) and a carboxylate group (COO-)

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3
Q

can amino acids be polar or non polar?

A

both

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4
Q

when is an amino acid nonpolar?

A

when the R group is H, alkyl, or aromatic (ex: attached to benzine ring or chain of carboxyl groups)

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5
Q

when is an amino acid polar?

A

when the R group is an alcohol, a thiol, or an amide (ex: anything with Oxygen or SH or O=C-NH2 at the end)

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6
Q

what is sickle-cell anemia caused by? What does it cause to happen?

A

an abnormality in one of the subunits (an amino acid) of the hemoglobin protein. This changes the shape of the blood cell to change form like a sickle shape, leaving it unable to adequately transport oxygen

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7
Q

what building blocks are proteins made of?

A

amino acids

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8
Q

are nonpolar amino acids water soluble? what’s the name for this?

A

no; hydrophobic

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9
Q

are polar amino acids water soluble? what’s the name for this?

A

yes; hydrophilic

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10
Q

what makes a polar amino acid neutral, acidic, or basic?

A

Neutral: contains neutrally charged ions in the R group of the amino acid
Acidic: contains negatively charged oxygen in the R group of the amino acid (a carboxylic acid)
Basic: contains positively charged Nitrogen in the R group of the amino acid (an amine)

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11
Q
A
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12
Q

are the alpha amino acids chiral or achiral?

A

all a-amino acids are chiral with exception for glycine

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13
Q

how do you tell if you are looking at the L or D enantiomer of a amino acid?

A

L: NH3+ appears on the left
D: NH3+ appears on the right

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14
Q
A
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15
Q

what are essential amino acids?

A

amino acids that cannot be produced in the body and need to come from our diet

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16
Q

what are examples of foods that contain complete proteins of all the essential amino acids?

A

meat, milk, eggs and fish

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17
Q

what are examples of foods that contain incomplete proteins of only some of the essential amino acids?

A

grains, beans, and nuts

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18
Q
A
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19
Q
A
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20
Q

amino acids can exist as positive ion or negative ion, how would you know which is it?

A

positive ion: if a solution is more acidic; lower pH than its pI
negative ion: if a solution is more basic; higher pH than its pI

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21
Q

what is the definition of pI?

A

Isoelectric point: when an amino acid with positive and negative charges is overall neutral in charge

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22
Q

would this have a pH higher or lower than 6?

A

lower than 6

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23
Q

what is another name for peptide bonds?

A

amide bonds

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24
Q

what is a peptide?

A

linking of two or more amino acids via peptide (amide) bonds

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25
Where does a peptide (amide) bond form?
between one amino acid's COO- group and another amino acid's NH3+ group gets ride of a water molecule (one oxygen from the COO- and two hydrogens from the NH3+)
26
what is the name of two/three/four amino acids bonded by peptide bonds?
dipeptides tripeptides tetrapeptides
27
28
what is the name of the reaction that forms di/tri/tetrapeptides?
amidation reaction
29
Since amino acids are the building blocks of proteins, how many amino acids does it take to form a functioning protein?
a protein is a polypeptide of 50 or more amino acids
30
which protein was the first to have its primary structure determined?
insulin
31
what does the primary structure of insulin contain?
two polypeptide chains linked by disulfide bonds
32
how many amino acids are used to build proteins in the body and how many can be synthesized within it?
20 11 9 are essential amino acids that are obtained through diet
33
what is the difference in appearance between primary and secondary structures of polypeptides?
primary: straight line secondary: helix spiral or pleated sheet
34
what are the differences of types of bonds found in primary vs secondary structures?
primary: only peptide bonds secondary: peptide and hydrogen bonds
35
where do hydrogen bonds form within the helix structure?
between the oxygen of C=O groups and the hydrogen of N-H groups of the amide bonds
36
what holds the chains together within a triple helix? what important function does this have?
hydrogen bonds added strength (as in with collagen and connective tissue)
37
which amino acids will have salt bridges in tertiary structures?
only ones with positive NH3+ bonds
38
what are examples of triple helixes in proteins? what type of structure are they?
collagen, connective tissue, skin, tendons, and cartilage secondary struture
39
what vitamin is important for the production of collagen?
vitamin C
40
what are the five characteristics of tertiary proteins?
hydrophobic interactions hydrophilic interactions salt bridges hydrogen bonds disulfide bonds
41
where do hydrophobic interaction occur within tertiary proteins? polar or nonpolar?
between two nonpolar amino acids at the center of the protein molecule
42
where do hydrophilic interactions occur within tertiary proteins?
between the external aqueous environment and the R groups of the polar amino acids
43
where do salt bridges occur within tertiary proteins?
between ionized R groups of basic and acidic amino acids (NH3+)
44
where do hydrogen bonds occur within tertiary proteins?
between H of a polar R group and the O or N of another amino acid
45
where do disulfide bonds occur between tertiary proteins?
between the SH groups of cysteine amino acids
46
myoglobin is a ___________ structure protein
tertiary
47
hemoglobin is a ____________ structure protein
quaternary
48
what force is important in the primary structure of a protein?
peptide bond
49
a-helix and b-sheet are in the ________ structure category of proteins?
secondary
50
which amino acid forms disulfide bonds to stabilize the tertiary structure of a protein?
cysteine
51
quaternary structure are made up of?
two or more protein subunits
52
hemoglobin is made up of what?
two a-chains and two b-chains
53
what kind of interactions are found in quaternary structures?
the same ones as with tertiary structures (hydrophilic/phobic, salt bridges, hydrogen bonds, and disulfide bonds
54
when does denaturation occur within proteins?
when there is a change that disrupts the interactions that stabilize the secondary, tertiary, or quaternary structure
55
Under what conditions can denaturation of proteins occur?
heat, organic compounds, acids and bases, heavy metals, and mechanical agitation (such as whipping a solution)
56
the cooking of an egg is an example of ?
denaturation
57
what are the bonds divided when heat is applied to proteins?
hydrogen bonds and hydrophobic interactions
58
what are the bonds disrupted when acids or bases denature proteins?
hydrogen bonds between polar R groups (salt bridges are disrupted)
59
what bonds are denatured when organic compounds are applied?
hydrogen bonds FORM and hydrophobic interactions are disrupted
60
what bonds are disrupted when heavy metals denature proteins?
disulfide bonds (instead it forms ionic bonds)
61
what bonds are disrupted when mechanical agitation denature proteins?
hydrogen bonds and hydrophobic interactions
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