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Biochem 1 > EXAM 2 > Flashcards

EXAM 2 Flashcards

1
Q

what is the distinguishing feature of amino acids?

A

the R functional group

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2
Q

what are the four components of an amino acid?

A

alpha carbon
amine group
carboxylic acid
R group

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3
Q

T/F hydrophobic amino acids have functional groups that only contain C’s and H’s

A

true

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4
Q

what are the 3 aromatic amino acids?

A

Tryptophan (trp)
Phenylalanine (phe)
Tyrosine (tyr)

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5
Q

what are the 3 branched amino acids?

A

leucine
isoleucine
valine

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6
Q

T/F hydrophilic polar charged amino acids have an additional acid/base functional group

A

True, there is an extra charge

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7
Q

what are the 2 sulfur-containing amino acids

A

cysteine
methionine

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8
Q

how many amino acids are there total

A

21

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9
Q

a compound that acts as both an acid and base

A

amphiprotic

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10
Q

what is a zwitterion

A

neutrally charged ion

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11
Q

what is the name of the bond between two amino acids

A

peptide linkage

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12
Q

what is a dipeptide

A

2 amino acids linked together

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13
Q

what is a tripeptide

A

3 amino acids linked together

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14
Q

what is a tetrapeptide

A

4 amino acids linked together

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15
Q

how many peptide bonds are within a tetrapeptide

A

3 peptide bonds

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16
Q

if you have 2 types of amino acids, how many different peptides can you make

A

4

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17
Q

if you have 3 types of amino acids, how many peptides can you make

A

27

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18
Q

T/F if you start with a molecule ABCDE. using hydrolysis you can make the molecule BCD

A

true

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19
Q

what is the energetic defining feature of the primary structure of a protein

A

covalent bond

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20
Q

T/F during denaturation, the primary structure remains uncharged

A

true

21
Q

with hydrolysis, are you adding water or removing it

A

adding water

22
Q

hat is the primary structure of a protein

A

amino acid sequence

23
Q

can you rotate a single bond

A

yes

24
Q

can you rotate a double bond

A

no

25
Q

what level of protein structure contains amide planes

A

secondary structure

26
Q

what causes the double helix

A

as the alpha carbon rotates, the amide planes run into one another

27
Q

how many AA residues are in one turn of an alpha helix

A

3.6

28
Q

is the alpha helix higher or lower in energy compared to the primary structure

A

lower in energy

29
Q

what is the tertiary structure of proteins

A

interaction of R groups

30
Q

what is the name of the bond between sulfur and sulfur

A

disulfide linkage

31
Q

what are the 4 types of bonds between tertiary structures

A

covalent bonds
hydrogen bonds
salt bridges
hydrophobic interactions

32
Q

which level of protein structure can change the binding site availability of proteins

A

quaternary structure

33
Q

what level of protein structure is the least stable

A

quaternary structure

34
Q

what levels of protein structure can be denatured

A

tertiary and quaternary structures

35
Q

what are the two methods of denaturation

A

temp and Ph

36
Q

what is myoglobin

A

oxygen-containing peptide

37
Q

where is myoglobin found

A

skeletal muscle

38
Q

are globular proteins water soluble

A

yes

39
Q

are fibrous proteins water soluble

A

no

40
Q

what are the functions of globular proteins

A

transporters
enzymes
immune globin
apolipoproteins receptors

41
Q

are tendons, ligaments, skin and collagen examples of fibrous proteins or globular proteins

A

fibrous proteins

42
Q

hat is the main AA in collagen

A

glycine

43
Q

collagen is made up of 33% __ and 22% ___

A

glycine, proline

44
Q

what is the result of not getting enough vitamin C

A

slow wound healing
gum bleeding
scurvy

45
Q

describe the bohr effect

A

if you increase the acidity, the capacity of binding oxygen decreases

46
Q

what counter balances the negative charge of HCO3 moving across the RBC barrier

A

Cl-, the chloride shift

47
Q

is oxygenated hemoglobin used in a venous vessel or an arterial vessel

A

venous vessel

48
Q

is deoxygenated hemoglobin used in a venous vessel or an arterial vessel

A

arterial vessel

Biochem 1 (1 decks)

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