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IB SL Bio > 2.4: Proteins > Flashcards

2.4: Proteins Flashcards

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Biology 101 flashcards
1
Q

how many amino acids are there in polypeptides synthesized on ribosomes

A

20 different amino acids

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2
Q

what bond links amino acids?

A

peptide bond

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3
Q

formation of a dipeptide

A

from amino acids

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4
Q

amino acid + amino acid –––––––>

A

dipeptide + water

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5
Q

characteristics of R group in amino acids

A
  • can be polar (hydrophillic)
  • can be non-polar (hydrophobic)
  • can be negatively or postively charged
  • can contain sulfur
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6
Q

what do characteristics of the R group do?

A

impacts the properties and behaviour of the protein

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7
Q

what do ribosomes do

A

they are the molecule within cells that facilitate the formation of peptide bonds and thus they are whwere polypeptides are synthesized

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8
Q

most organisms assemble polypeptides from the _________ amino acids

A

same

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9
Q

why are there infinite possibilities of polypeptides?

A
  • can be any length
  • 20 amino acids
  • amino acids in any order or combination
  • basically limitless
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10
Q

ribosomes aree the site of polypeptide synthesis, but ribosomes need a template– the ________________ which in turn, is ______________ by __________________ molecules, which, in turn, carry __________________.

A

messenger RNA
translated
transfer RNA
specific amino acids`

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11
Q

Genes are….

A

codes for making polypeptides

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12
Q

mRNA (messenger RNA) is…

A

a message from nucleus to ribosome
- gives intructions on how to put polypeptide together

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13
Q

genetic code is…

A

the sequence of bases on mRNA
- tells ribosome which amino acids to use

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14
Q

open reading frame

A

the base sequence that codes for polypeptide
- only occupy small portion of total DNA in species

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15
Q

lysozome

A
  • has one polypeptide
  • enzymes in secreted biody fluids kills bacterial by breaking down the peptidoglycan in their cell walls
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16
Q

collagen

A
  • has three polypeptides
  • strong, elestic structural protein found in connective tissues
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17
Q

hemogoblin

A
  • has four polypeptides
  • transport protein in red blood cells
  • binds oxygen from long and releases into tissues with lower oxygen concentration
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18
Q

polypeptides are the _______________ of protein structure

A

base or primary level

19
Q

how different amino acids interact with each other and their surrounding determines…

A

their 3d shape

20
Q

before polypeptides are functional they must…

A

fold into specific structures based on the order/ structure of their amino acid sequence

21
Q

primary protein structure

A

sequence of a chain of amino acids

22
Q

secondary protein structure

A

hydrogen bonding of the peptide backbone causes the amino acids to fold into a repeating pattern

23
Q

tertiary protein structure

A

three dimensional folding pattern of a protein due to side chain interactions

24
Q

quaternary protein structure

A

protein consiting of more than once amino acid chain

25
Q

shape: fibrous proteins vs globular proteins

A

fibrous proteins:
- long and narrow
globular protein:
- rounded/spherical

26
Q

role: fibrous proteins vs globular proteins

A

fibrous:
- structural
- strength and support
globular protein
- functional
- catalytic, transport etc

27
Q

solubility: fibrous protein vs globular protein

A

fibrous:
- generally insuluble in water
globular:
- generally soluble in water

28
Q

sequence: fibrous protein vs globular protein

A

fibrous:
- repetitive amino acid sequence
globular:
- irregular amino acid sequence

29
Q

stability: fibrous protein vs globular protein

A

fibrous:
- less sensitive to chnages in heat, pH etc
globular:
- more sensitive to heat, pH etc

30
Q

examples: fibrous protein vs globular protein

A

fibrous:
- collagen, myosin, fibrin, actin, keratin, elastin
globularL
- catalase, haemoglobin, insulin, immunoglobin

31
Q

The 3D conformation of protein is stabilized _____________________ between R groups of amino acids within the molecule

A

by bonds or interactions

32
Q

Most of these bonds are relatively weak, and can be _______________ with exposure to heat or changes in pH

A

disrupted or broken

33
Q

breaking or disrupting bonds results in a change to the ______________ of the protein, which is called __________ (usually permanent), this also causes a loss in ___________

A

conformation
denaturation
function

34
Q

renaturation

A

when protein regains its original 3D shape (and function)
- can happen if the exposure is minimal, and the factor removed after a short time

35
Q

temperature on denaturation

A
  • causes vibrations within the molecule that can break intermolecular bonds or interactions
  • Different proteins have different tolerances to heat
36
Q

pH on dentauration (too acidic or too basic)

A
  • Changes the charges on R groups, breaking ionic bonds within the protein or causing new ionic bonds to form
  • Different proteins have different optimal pH values
37
Q

rubisco

A
  • abbrev. for ribulose bisphosphate carboxylase
  • very important enzyme
  • catalyses reaction that fixes carbon fixes co2 from atmsophere
  • provides source of carbon that can produce carbon compounds
  • found in high concentration in leaves
38
Q

insulin

A
  • hormone that gives signal to cells in body to absorb/reduce/regulate glucose conc. in blood
  • cells have receptor to let insulin to bind to
  • insulin is secreted in beta cells in pancreas
39
Q

immunogoblin

A
  • aka antibodies
  • binds to antigens on bacteria/pathogens
  • casues response for phagocytes to engulf pathogens
  • basis for immunity to disease
40
Q

rhodopsin

A
  • a pigement that absorbs light for vision
  • contains light sensitive molecule surrounded by opsin polypeptide
  • when it absorbs a single photon of light, it chnages shape, causing opsin to also change shape, leading to impulse being sent to brain
41
Q

spider silk

A
  • conatains regions where polypeptides form parallel arrays
  • very exrensble and resistent to breaking
42
Q

proteome

A

all porteins made by a cell, tissue or organism

43
Q

genome

A

all the genes of a cell, tissue or organism

44
Q

proteome vs genome

A

proteomes are unique among individuals of same species, genome is not

IB SL Bio (37 decks)

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