amino acids + protein structure Flashcards

1
Q

a chain or amino acids is a

A

protein

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2
Q

what dictates the order of amino acids

A

genetic information of the cell (DNA)

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3
Q

what is the genetic information converted into and that does that do

A

it is converted to mRNA which is then used to create the protein

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4
Q

proteins are the ___ of the cell and perform ________ that give cells their properties

A

workhorses, specific functions

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5
Q

what do enzymes do

A

catalyze covalent bond breakagew

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6
Q

what do structural proteins do

A

provide mechanical support to cells and tissues

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7
Q

what do transport proteins do

A

carry small molecules or ions

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8
Q

what do motor proteins do

A

generate movement in cells and tissues

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9
Q

what do storage proteins do

A

store amino acids or ion

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10
Q

what do signal proteins do

A

carry extracellular signals from cell to cell

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11
Q

what do receptor proteins do

A

they detect signals and transmit them to the cell’s response machinery

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12
Q

what are transcription regulators

A

they bind to DNA to switch genes on or off

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13
Q

what are special purpose proteins

A

high variable with specialized properties (could be anti freezing etc. )

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14
Q

what are antibodies composed of

A

four peptide chains - two identical light chains and two heave chains

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15
Q

what are the chains of antibodies help together by?

A

disulfide bonds

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16
Q

what do neutralizing antibodies do

A

they bond to virus

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17
Q

what do antibodies block

A

surface proteins, and important binding protein

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18
Q

what does a positive or negative amino acid mean

A

they are charged which means they are strongly hydrophilic or water loving

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19
Q

which amino acids are positive

A

ones with a nitrogen group but no oxygen (arginine, histidine, and lysine)

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20
Q

which amino acids are negative

A

ones with an extra carboxyl group (aspartic acid and glutamic acid)

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21
Q

which amino acids are hydrophilic but not charged

A

amino acids that are polar due to OH, or nitrogen groups with oxygen (serine, threonine, asparagine, glutamine, and tyrosine)

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22
Q

what are the expectations to the amino acids that are generally hydrophobic

A

cysteine: CH2-SH, glycine: H, proline: ring of 3 C from central C no amine

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23
Q

which amino acids are nonpolar hydrophobic side chains

A

ones with just C, H for the most part, methionine has S and tryptophan has N (alanine, isoleucine, leucine, methionine, phenylalanine, tryptophan, and valine)

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24
Q

which amino acid does every protein start with

A

methionine

25
what is the average length of a protein
500 amino acids
26
the ______ of amino acids dictates protein ______
sequence, shape
27
How does the amino acid sequence influence 3D shape
it drives the interactions with water and intramolecular bonding of the linear amino acid chain
28
which sides of the chains can form hydrogen bonds to water
polar side
29
which sides of the chains are packed into the hydrophobic core region
nonpolar
30
what are the four levels of protein structure
primary, secondary, tertiary, quaternary
31
what is the primary level
amino acid monomers are joined which forms polypeptide chains
32
what type of bond stabilizes the primary level
peptide bonds
33
what does the primary level dictate
intramolecular interactions
34
what is the secondary level
the polypeptide chains may form alpha helices or beta pleated sheets
35
what do the secondary and tertiary levels dictate
shape
36
what types of bonds stabilize secondary level
hydrogen bonds
37
how does a protein fold into a repeating pattern
through hydrogen bonding between atoms in the peptide backbone
38
What is hydrogen bonded together in an alpha helix
the N-H of every peptide bond and the C=O of a neighboring peptide bond located four amino acids away in the same chain
39
what types of interactions occur between atoms in the peptide backbone only of alpha helices
noncovalent
40
what are beta sheets
they are several segments (strands) of an individual polypeptide chain that are help together by hydrogen bonding in adjacent strands
41
describe the strand shape of beta sheets
each strand projects alternately above and below the plane of the sheet
42
what type of interactions occur in beta sheets
noncovalent that are occurring between atoms in the peptide backbone only
43
what is the tertiary level
polypeptides fold which forms specific shapes. largely determined by interactions between R-groups
44
what type of bond stabilizes the tertiary level
hydrogen bonds, disulfide bons, and hydrophobic interactions
45
what are disulfide bonds/bridges
two cysteines that lose their H and connect at their sulfur groups
46
where do ionic interactions/salt bridges form (electrostatic interactions
between charged amino acid side chains
47
what is the exception to the clumping of hydrophobic amino acids inward to the center (Vander waals attractions)
membrane proteins
48
what type of bond occurs between a hydrophilic side of a chain and a backbone of another chain
hydrogen bonds
49
backbone to backbone
hydrogen bond between atoms of two peptide bonds
50
backbone to side chain
hydrogen bond between atoms of a peptide bond and an amino acid side chain
51
side chain to side chain
hydrogen bond between atoms of two amino acid side chains
52
what happens with membrane proteins
the hydrophobic side chains of the amino acids make contact with the hydrophobic hydrocarbon tails of the phospholipid molecules
53
what is a protein domain
is it a distinct, compact, and independently folding structural unit within a protein molecule. It is a subunit of a tertiary structure.
54
_____ are functional and often have __________ within the larger protein structure
protein domains, specific roles
55
what is quaternary structure
two or more polypeptides assemble to from larger protein molecules
56
what stabilizes quaternary structure
noncovalent bonds (hydrogen bonds, hydrophobic, ionic) and disulfide bridges-same as tertiary structures
57
what are possibilities of misfolded proper protein folding
degenerative and neurovegetative such as (Alzheimer's, Parkinson's, Huntington's, ALS)
58
what are chaperones
they help proteins fold properly
59
what does ubiquitin do
it marks a cell to target them to the proteosome for degradation