ch.6 Flashcards

(49 cards)

1
Q

what is the basic structure of an amino acid

A

all 20 amino acids share a common structure: alpha carbon connected to an amino group and a carboxyl group

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2
Q

how do amino acids differ from one another

A

they differ in the variable associated side chain (R)

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3
Q

what are the three forms of amino acids

A

alpha, beta, gamma

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4
Q

what defines an alpha amino acid

A

always the one bonded to the carboxyl group

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5
Q

what characterizes a beta amino acids

A

a second carbon is bonded to the amino group

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6
Q

what is an example of a gamma amino acid

A

Gamma-aminobutyric acid (GABA) is a gamma amino acid that functions as a neurotransmitter

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7
Q

what is the role of GABA in the body

A

responsible for inhibition of neuron firing and is the most abundant neurotransmitter in the body

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8
Q

which isomer of amino acids is primarily used as building blocks of proteins

A

only the L isomers are used as building blocks of proteins

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9
Q

why are some amino acids considered biological buffers

A

maintain the narrow pH range of cells (7.35-7.45)

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10
Q

what happens to amino acids at low pH

A

the carboxyl and amino groups accepts a proton and become protonated

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11
Q

what occurs to amino acids at high pH

A

the amino and carboxyl group donate a proton and become dissociated

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12
Q

what is a zwitterion

A

can donate or gain a proton and has both negative and positive groups

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13
Q

what are the three classes of amino acids based on their chemical properties

A
  1. nonpolar (neutral)
  2. polar (made of atoms that are very electronegatively different)
  3. charged (contain a charge on the R group)
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14
Q

what are some examples of nonpolar amino acids

A
  • leucine
  • isoleucine
    -methionine (Met)
    -Tryptophan (Trp)
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15
Q

what are essential amino acids

A

those that an animal cannot synthesize in sufficient amounts and must be obtained from the diet

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16
Q

how many essential amino acids are there for adult humans

A

8

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17
Q

what are the 8 essential amino acids

A
  1. tryptophan
  2. methionine
  3. valine
  4. threonine
  5. phenylalanine
  6. leucine
  7. isoleucine
  8. lysine
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18
Q

how are amino acids linked together to form a polypeptide

A

via peptide bonds

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19
Q

what forms the polypeptide backbone

A

the repeating structure of atoms forms the polypeptide backbone with side chains coming out of it

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20
Q

what are the end of a polypeptide called

A

have an N-terminus (free amino end) and C-terminus (free carboxyl end)

21
Q

what is a protein

A

one or more polypeptides twisted, folded and coiled into a unique shape

22
Q

how does the sequence of amino acids affect a protein

A

determines a protein’s three-dimensional structure, which in turn determines its function

23
Q

what are the four levels of protein structure

A
  1. primary
  2. secondary
  3. tertiary
  4. quaternary
24
Q

what is the primary structure of a protein

A

the specific and unique sequence of amino acids that composes a polypeptide, determined by the nucleotide sequence of the gene that encodes the protein

25
what holds the primary structure of a protein together
peptide bonds
26
what characterizes the secondary structure of a protein
involves coiling and folding of the polypeptide chain stabilized by hydrogen bonds between amino group and carboxyl groups
27
what are the two common forms of the secondary structure
alpha helix and beta pleated sheets
28
what is alpha helix
coiled structure held in shape by hydrogen bonds common in fibrous proteins
29
what is beta pleated sheet
structure where hydrogen bonds hold neighboring strands of sheet together, common for globular proteins
30
what determines the tertiary structure of a protein
overall 3D shape resulting from interactions among the R groups
31
what are the four possible interactions that determine tertiary structure
1. hydrogen bonds 2. hydrophobic interactions 3. disulfide 4. ionic bonds
32
what characterizes globular proteins
compact combinations of alpha helix and beta pleated sheets, forming a spherical shape
33
what characterizes fibrous proteins
mostly alpha helix and have a straight (ish) structure
34
what is the quaternary structure of a protein
association of multiple polypeptide chains formed by interactions among the chains that comprise the protein
35
do all proteins have a quaternary structure
no
36
what is hemoglobin
a globular protein with four polypeptide subunits
37
what is collagen
a fibrous protein consisting of three helical polypeptides coiled together
38
how does a change in primary structure affect protein function
even a small change in primary structure can alter the protein's conformation and ability to function
39
what is sickle cell disease
sickle cell disease occurs when a negatively charges amino acid is replaces by a non-polar one, altering protein folding and blood cell shape
40
what is the function of molecular chaperones in cells
chaperonins separate new polypeptides from potentially disruptive chemical conditions within the cytoplasm and help them fold into their correct shape
41
what are the two types of proteins based on polypeptide composition
1. monomeric: made up of one polypeptide chain 2. oligomeric: consist of two or more polypeptide chains
42
what are the two types of proteins based on composition
1. simple protein: only made up of amino acids 2. conjugated protein: contain amino acids and some other chemical group (organic molecule or metal ion)
43
what are prions
misfolded proteins that have become infectious agents
44
what diseases are associated with prions
affect the structure of the brain or neural tissue and are currently untreatable and always FATAL
45
what are prion diseases collectively called?
spongiform encephalopathies
46
what causes prion diseases
the dysfunctional version of the protein interacts with the normal version
47
what is denaturation of a protein
disruption and possible destruction of secondary, tertiary and sometimes quaternary structures but DOES NOT DISTURB PRIMARY STRUCTURES
48
what environmental conditions can promote denaturation
heat, extreme pH. and alcohol can promote denaturation of proteins
49
what are some diseases associated with protein denaturation
1. Alzheimer's: characterized by protein plaques and neurofibrillary tangles in the brain 2. Cancer: often caused by misfolding of proteins that function as tumor-suppressor agents