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bio module 2 > proteins > Flashcards

proteins Flashcards

1
Q

elements in proteins?

A

C H O & N

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2
Q

“peptide” definition

A

polymers made of amino acid molecules (monomers) with specific biological functions

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3
Q

amino acid structure?

A

centre carbon
- R group
- amine group (NH2)
- H
- carboxyl group (COOH)

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4
Q

what makes amino acids different?

A

different R groups

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5
Q

how many amino acids are commonly found in cells?

A

20

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6
Q

how many amino acids are essential & non-essential & conditionally essential?

A

essential = 9
non-essential = 5
conditionally essential = 6

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7
Q

what are conditionally essential amino acid?

A

only needed in growing children

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8
Q

when do amino acids join?

A

when the amine and carboxylic acid groups connected to central carbon react

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9
Q

how do amino acids react with each other?

A

peptide bond formed + water produced

when hydroxyl of one amino acid reacts w hydrogen of another

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10
Q

what type of reaction is amino acid synthesis?

A

condensation reaction

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11
Q

what bond forms between amino acids?

A

peptide bonds

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12
Q

polymer of amino acids?

A

polypeptide

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13
Q

monomer of polypeptides?

A

amino acids

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14
Q

enzyme catalysing polypeptide synthesis?

A

peptidyl transferase (ribosomes)

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15
Q

where is the enzyme for polypeptide synthesis found?

A

peptidyl transferase in the ribosomes

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16
Q

how do amino acid chains fold into proteins?

A

bonds formed by amino acid R groups

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17
Q

what do different amino acids do for protein structure?

A

diff amino acids fold polypeptide chains into different proteins w/ different shapes

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18
Q

“primary protein structure”

A

the sequence in which amino acids are joined

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19
Q

what bonds are involved in primary protein structure?

A
  • peptide bonds
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20
Q

“secondary protein structure”

A

O H & N of basic repeating amino acid structures interact, forming H bonds between amino acids = a helix or b pleated sheet structures

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21
Q

a helix structure

A

hydrogen bonds within amino acid chain pull into coil shape

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22
Q

b pleated sheet

A

polypeptide chains lie parallel to each other joined by hydrogen bonds = sheet like structures

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23
Q

what bonds are involved in secondary structure?

A

hydrogen bonds (+ peptide primary)

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24
Q

“tertiary protein structure”

A

how the folding of secondary structure into protein brings R groups close via disulfide bridges, ionic bonds, hydrogen bonds & hydrophobic hydrophilic interactions to form a 3D structure

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25
what bonds are involved in tertiary protein structure?
- h bonds (weakest) - ionic bonds (between opp charged R groups) - disulfide bridges (covalent + strongest but only between sulfur containing R groups) - hydrophobic philic (weak polar non-polar interactions)
26
tertiary hydrogen bonds?
weakest bonds
27
tertiary ionic bonds?
between opp charged R groups
28
tertiary sulfide bridges?
covalent + strongest bonds between sulfur containg R groups
29
tertiary hydrophobic hydrophilic interactions?
**weak interactions** between polar & non-polar R groups
30
“quaternary protein structure”
result of association of 2+ individual proteins (subunits) aka tertiary structure bonds between proteins not R groups
31
“subunits”
individual proteins
32
how many subunits does insulin have?
2 identical subunits
33
how many subunits does haemoglobin have?
2 different sets of 2 identical subunits
34
where are protein hydrophilic groups?
outside (cytoplasm)
35
where are protein hydrophobic groups?
inside (away from cytoplasm water)
36
reaction breaking peptides down?
hydrolysis
37
“dipeptide”
product of 2 amino acids joined (monomers)
38
“tripeptide”
product of 3 amino acids joined together (monomers)
39
“polypeptide”
polymer produced when many amino acids (monomers) are joined together
40
“amphoteric” (amino acids are [] )
molecule that acts as base and acid
41
“amorphous regions”
regions without a helixes or b pleated sheets in secondary structure
42
“globular proteins”
compact, water soluble molecules with chemical properties
43
globular protein characteristics
- compact - water soluble - spherical
44
why are globular proteins water soluble?
tertiary structure where hydrophobic R groups inside + hydrophilic R groups outside
45
why is globular protein solubility important?
regulating processes - eg. chemical reactions - immunity - muscle contractions etc
46
“insulin” definition
globular protein hormone involved in regulating blood glucose levels
47
why do hormones need to be soluble?
transported in blood stream
48
how do hormones need precise shapes?
need to fit specific receptors on cell surface membranes for effect
49
“conjugated protein” definition
globular protein contains a non-protein component (prosthetic group)
50
“prosthetic group”
non-protein component
51
“simple protein” definition
protein not containing a prosthetic group
52
are lipids / carbohydrates prosthetic groups?
yes
53
what are lipoproteins?
lipid (pros group) + protein
54
what are glycoproteins?
carbohydrate (pros group) + protein
55
what can form prosthetic groups?
- lipids - carbs - metal ions - molecules derived from vitamins **- haem groups containing Fe2+**
56
what molecules have haem groups?
- haemoglobin - catalase
57
what is haemoglobin?
red, oxygen-carrying pigment found in RBCs
58
what is the structure of haemoglobin?
quaternary protein of four polypeptides - 2 alpha subunits - 2 beta subunits
59
how many subunits in haemoglobin and what do they contain?
2 alpha + 2 beta - each has a prosthetic haem group
60
what allows haemoglobin to take up and transfer oxygen?
Fe2+ ions in haem group bind reversible with O2 molecules = carried for transportation from lungs to cells
61
“catalase”
enzyme containing 4 haem prosethic groups that catalyses breaking down in metabolism
62
“enzyme” definition
catalyse and speed up rate of reaction by introducing alternate reaction pathway without being used up themselves specific to a reaction
63
structure of catalase?
quaternary protein with 4 prosthetic haem groups
64
reason for haem groups in catalase?
4 haem groups - Fe2+ ions allow catalase to interact with hydrogen peroxide and speed up break down
65
what is hydrogen peroxide?
byproduct of metabolism damaging to cells and cell components if allowed to accumulate
66
“fibrous proteins”
formed from long, insoluble molecules due to high proportion of hydrophobic R group in primary structure proteins
67
fibrous protein structure?
- limited range of amino acids - small R groups - repetitive amino acid primary structure sequence = organised structure - strong long molecules NOT FOLDED INTO 3D SHAPES like globular proteins
68
why do fibrous proteins have an organised structure?
repetitive primary structure amino acid sequence
69
fibrous protein examples? where are they found?
- keratin (hair skin nails) - elastin (blood vessels alveoli in lung) - collagen (muscles bones tendons ligaments)
70
“keratin”
fibrous protein in hair, skin and nails with large proportion of sulfur containing amino acids
71
keratin characteristics?
- strong - inflexible - insoluble
72
what does keratin have its characteristics?
disulfide bonds = strong, inflexible, insoluble less bonds (hair) = more flexible
73
keratin bonds?
disulfide bonds - more (nails) = less flexible than less (hair) = flexible
74
what is the smell when hair / skin is burnt?
burning of sulfur
75
“elastin”
fibrous protein found in elastic fibres allowing for stretching and returning to original size
76
where are elastic fibres found?
blood vessel walls & alveoli of lungs
77
elastin structure?
quaternary protein made of tropoelastin (stretchy molecules)
78
benefits of elastin?
allow structures to expand flexibly and return to original shape
79
“collagen”
fibrous protein connective tissue found in skin, tendons, ligaments, nervous system
80
collagen characteristics?
- strong - flexible
81
why are collagen’s characteristics like that?
Wound of 3 polypeptides wound together in long, rope-like structure

bio module 2 (7 decks)

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