2.4 proteins Flashcards

1
Q

what are proteins?

A

proteins are POLYMERS made from AA (which are the monomers)

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2
Q

what determines the properties of proteins?

A

determinded by the R group on the AA
H
l
amino group – C – carboxyl group
(NH2) l (COOH)
R

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3
Q

How many common (made by ribosomes) AA are there

A

20

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4
Q

RECALL HOW TO DRAW PEPTIDE BOND FORMATION

A

carboxyl grp from AA + amino grp from AA – dehydration recation –> peptide bond between C=O and N-H + H2O

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5
Q

how are amino acid polypeptide sequences arranged

A
  • prod in ribosomes
  • AA linked tgt in sequence dictated by genes (sequences of DNA carrying info for expression)
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6
Q

what are the bare bones of the process from DNA to polypeptide production

A

DNA –transcription–> RNA –translation–> polypeptide

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7
Q

what is the start codon?

A

AUG

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8
Q

What are the stop codons

A

UAA
UAG
UGA

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9
Q

what are the 4 levels of protein structure?

A
  • primary
  • secondary
  • tertiary
  • quaternary
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10
Q

what is primary protein structure

A

a sequence of AA along the polypeptide chain (w peptide bonds), determined from genetic info

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11
Q

what is secondary structure of a protein

A
  • parts of polyp chain COIL onto itself, forming ALPHA HELICES
  • other parts can fold into BETA PLEATED STRUCTURE
  • stabilised by HYDROGEN BONDS btw AA
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12
Q

what is tertiary protein structure

A
  • overall THREE DIMENSIONAL SHAPE of a protein
  • from bonds formed between R groups
  • eg. disulphide bridge betw 2 sulfur-containing AAs
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13
Q

what is quarternary structure of protein

A
  • when 2 OR MORE polypeptide chains ASSOCIATE to form resultant protein
  • not all proteins
  • eg collagen (triple helix), haemoglobin (4 polyp chains)
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14
Q

are all enzymes proteins?

A

no! some enzymes are made of RNA.

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15
Q

protein function: enzymatic

A

its just an enzyme man cmon lock and key
substrate in active site then products

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16
Q

proetin function: storage, 2 examples

A

examples
- egg albumin
- casein in milk (makes it white)

17
Q

protein functions: hormonal, 3 ex

A
  • insulin
  • glucagon
  • adrenaline
18
Q

protein function: contractile and motor, 2 ex

A

both found in muscle cells
- actin
- myosin

19
Q

protein functions: defensive, 1 ex

A

antibodies – clump onto bacteria

20
Q

protein functions: transport, 1ex

A

electron transport chain proteins

21
Q

protein functions: receptor

A

on plasma membrane, receives signal molecule –> relay molecules –> response

22
Q

protein function: structural, 1 ex

23
Q

define PROTEOME

A

the sum of all proteins that can be produced by the species

24
Q

define GENOME

A

the sum of all genes encoded within the DNA of that species

25
what is the proteome dependent on?
- genome of the species - environment
26
rubisco full name
ribulose bisphosphate carboxylase
27
what does rubisco do? 2
it is an ENZYME - used to FIX CO2 from atmos (part of calvin cycle) - provides SOURCE of carbon during psis + formation of complex C compounds
28
where is rubisco found?
its an ENZYME found in high conc in leaves of plants
29
what is insulin?
a hormone, used to reg blood glucose levels -- secreted in response to HIGH glucose levels, prod by pancreas
30
what are immunoglobins 3
- also known as antibodies - 2 antigen binding sites per protein - diff antibodies have diff antigen binding sites -- specific - can also bind to antigens on bacteria
31
what do antibodies bind to?
ANTIGENS
32
what do antibodies do to bacteria
AGGLUTINATE - not able to cause infections - clumped tgt = engulfed by WBC (phagocytosis)
33
what is rhodopsin?
its visual purple 💜💜💜 - pigment that can absorb light - found in receptor cells in retina
34
what happens when a photon reaches a rhodopsin molecule?
isomerisation occurs -- change in molecule shape
35
what is collagen?3
- structural protein, TRIPLE HELIX - forms a mesh = resistance against tearing and shearing - structural strength
36
spider silk as a protein ??
- what it says on the tin. forms webs - fibres can extend when streched - stronger than steel cables
37
denaturation of proteins by HEAT 3
1. heat energy incr vibration of atoms 2. vibration breaks weak internal bonds 3. affects 3d shape low -- low activity high -- denatured
38
denaturation of proteins by pH 3
1. extreme pH changes CHARGES of R GRPS 2. breaking of ionic bonds 3. changes to protein shape low/high -- dentaured