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Biology IB > B1.2: Proteins > Flashcards

B1.2: Proteins Flashcards

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1
Q

Monomers of proteins?

A

Amino acids.

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2
Q

How many amino acids are there?

A

20 amino acids only

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3
Q

Which organelle produces proteins

A

Ribosomes

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4
Q

Why do we still need to consume meat/soya for protein if we have a lot of them due to ribosomes?

A

We don’t have all types of amino acids, therefore, they need to be supplemented via meat or soya, etc.

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5
Q

Define muscle wasting (DOUBLE CHECK)

A

the wasting (thinning) or loss of muscle tissue
- when proteins as a source of energy when carbs and lipids aren’t there

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6
Q

Outline the two types of amino acids

A

Essential and non-essential

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7
Q

Define essential proteins

A

Protein from other organism

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8
Q

Define non-essential proteins

A

Come from our body (thus it’s not essential to consume from external sources)

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9
Q

What are a 2 amino acids tgt called?

A

Dipeptide

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10
Q

Outline the sequence of complexity

A

amino acid (monomer) -> dipeptide -> polypeptide -> proteins

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11
Q

Define denatured on terms of proteins

A

The (natural quality which is specifically:) functional shape of protein is disrupted

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12
Q

Outline the different structures found in an amino acid

A

Amine grp (NH2)

Carboxyl grp (COOH)

Hydrogen atom (H)

Variable side chain (R)

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13
Q

What is the chemical composition of proteins?

A

CHON/S
(Carbon, Hydrogen, Oxygen, Nitrogen and with or without?? Sulfur)

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14
Q

Draw the structure of a generalised amino acid

A

(no need to draw a box)

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15
Q

What is the bond between protein?

A

Peptide bond

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16
Q

What makes an amino acid different from eachother

A

Their R (variable side chain)
- determines type of protein (polar or non-polar)

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17
Q

What determines the charge of the amino acid/protein?

A

The R

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18
Q

Describe the folding of long amino acid chains

A

The R’s can be attracted to each other and thus “fold” the chain which affects the structure and function

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19
Q

Most natural polypeptide chains contain between how many amino acid residues?

A

50 - 2000

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20
Q

Describe peptide bonds

A
  • covalent bond
  • condensation to dipeptide and water
  • broken by hydrolysis (?)

(between C and N — the one in green. btw they bind at one’s carboxylic group and amine group)

21
Q

amino acid + amino acid —> ?

A

dipeptide + water

22
Q

Outline the types of structure in proteins

A

1.) Primary
2.) Secondary
3.) Tertiary
4.) Quaternary

23
Q

Describe the primary structure of amino acid

A

Purely the sequence/arrangement

e.g.: Amino acid 1 - amino acid 2 - amino acid 3 - …

24
Q

Describe the secondary structure

A

Folding (depends on R)
- Two stable forms:
1.) B (beta)-pleated
2.) A (Alpha)-helices (helical)

  • both result from hydrogen bonds (and peptide) between amino acids
  • Bonding of amino acids not to the neighbor - non-adjacent
25
Q

Describe the B-pleated secondary structure (CONT.)

A

It consists of various beta strands linked by hydrogen bonds between adjacent strands.
- Unique folding (zigzag)

26
Q

Define helical bond in the secondary structure

A

Circular

27
Q

Describe the tertiary structure of the protein

A

Determined by the interactions between the R chains
- 3D configuration
- hydrophobic inside; hydrophilic outside

28
Q

Describe quarternary structure

A

Made up of different polypeptides folded to one another with diff. prosthetic grps
e.g.: tertiary and tertiary, tert and secondary, quarternary and..

29
Q

Define denaturation

A

a structural change that results in the loss of its biological properties
- additionally, can also break bonds

30
Q

What is the denaturation of proteins caused by?

A

Temp and pH

31
Q

Describe tertiary structure

A

R side groups bond tgt, 3D Configuration/Arrangement
- (relation to the R groups and 3D-ness): Polar amino acids stick outside whereas non-polar amino acids hide inside

32
Q

Where do peptide bonds form?

A

Carboxyl group and Amine group by condensation

(removal of the OH from the carboxyl group and the H atom from the amine group of another amino acid -> water byproduct -> allows one more bond for the carbon and nitrogen to create a peptide bond!)

33
Q

Why are prosthetic groups not the same as the R group

A

Prosthetic groups are not part of the amino acid
- R group is pat of the amino acid, therefore, not part of the amino acid
- But prosthetic groups, despite not being an amino acid, are bonded to the polypeptides in quaternary structures

34
Q

Outline the two types of proteins according to structure and function

A

1.) Globular, functional (reactions) — round
- e.g. enzymes

2.) Fibrous, on structure — long and thin

35
Q

Outline the two causes of denaturation of proteins

A

1.) Temperature
2.) PH level

36
Q

Why is protein sensitive to temperature?

A

High thermal energy can disrupt the hydrogen bonds that hold the protein together (2nd structure)
- Also note: peptide bond within amino acid, hydrogen bond between amino acid (like covalent bonds and hydrogen bonds in water)
- will cause protein to unfold and therefore not function

37
Q

Why is protein sensitive to pH

A

amine grp and carboxyl grp not bonding tgt, attracted to other atoms (H if more acidic and OH if more alkaline)
- thus, it’ll alter the shape of the protein (primary structure?) -> protein shape and protein solubility (-> function?)

38
Q

What determines the type of protein?

A

By the sequence of genes (Translation)
- usually 1 gene 1 protein type??, e,g, 1 gene -> hair color (DOUBLE CHECK)
- But the grouping of genes to proteins is different due to translation (ADD PHOTO)

e.g.: The reason why some people are lactose-intolerant is that their genes have “turned off” the lactose-tolerating proteins (? DB)
The genes determine the hair-color

39
Q

Define proteome

A

total proteins expressed with a cell, tissue, organism at a certain time

40
Q

Which do we have more of? Proteins or genes?

A

Proteins > genes

41
Q

Explain the 1 gene to 1 protein type ratio

A

1 gene -> 1 type/purpose (e.g. hair color) -> different variations of proteins (e.g. brown blue and green in one person
- The proteome depends on the expression of proteins (dom vs recess.)

42
Q

Describe fibrous proteins

A
  • Long, narrow
  • Structural

-Repetitive amino acid sequence

  • Less sensitive to changes in pH and temp, etc.
  • Generally insoluble in water

e.g.: collagen, myosin, fibrin. actin and keratin, etc.

43
Q

Describe globular proteins

A
  • Round/spherical
  • Functional
  • Irregular amino acid sequence
  • More sensitive to changes in pH, temp. etc. (they have optimum pH level and temp for chem reactions — enzymes)
  • Generally soluble in water (ig related to the chemical reaction function??)

e,g, enzymes

44
Q

Give the function of the enzyme Rubisco

A

Catalyzes photosynthesis — carbon-fixation
- fixes carbon dioxide from the atmosphere — provides carbon needed by living organisms

45
Q

Give the function of the hormone Insulin

A

Lowers blood glucose levels

46
Q

Give the function of the structural protein, Collagen

A

To prevent skin tearing by wounding three polypeptides in a rope-like way.
- (which is why you oft see collagen in shampoo ads)

47
Q

Give the function of the antibody, immunoglobulin

A

bind to antigens (substances that illicit a bodily reaction) in pathogens

48
Q

Give the function of the pigment Rhodopsin

A

makes the rod cells of the retina light-sensitive

49
Q

Which atom makes a bond covalent?

A

Oxygen — has electrons for electron sharing (covalent bond)

Biology IB (32 decks)

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