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FND 100 Final > FND 100 Proteins > Flashcards

FND 100 Proteins Flashcards

1
Q

What percent of caloric intake do proteins contribute to?

A

20% of total caloric intake

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2
Q

How much of your plate should contain proteins?

A

1/4 of a plate serving for protein recommendations

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3
Q

What is part of the protein recommendations in Canada’s Food Guide?

A

Part of the recommendation for encouraging the consumption of more plant based proteins because they are related to reduction of chronic disease rates

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4
Q

Benefits of proteins?

A

Dietary fibre and other dietary components
Reductions in plasma cholesterol (LDL cholesterol), reductions in colon cancer, type two diabetes linked in increased consumption of protein

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5
Q

Proteins and muscles

A

Muscle structure is a protein and involved in physiological of actin myosin complex

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6
Q

What are examples of structural proteins?

A

Keratin
Actin/myosin complex

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7
Q

What are examples of biologically functional proteins and peptides?

A

Enzymes
Hormones
Growth factors
Trypsin inhibitor
Peptides

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8
Q

What are biologically functional proteins also known as?

A

Bioactive proteins

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9
Q

Examples of biologically functional proteins: enzymes

A

Salivary amylase, proteases, enzymatic browning, lysozyme (unique to egg white break apart microbes to protect interior of egg)

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10
Q

Examples of biologically functional proteins: hormones

A
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11
Q

Examples of biologically functional proteins: growth factors

A

Cancer cells which contain growth factors that influence cancer cell growth

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12
Q

Examples of biologically functional proteins: trypsin inhibitors

A

Important in the context of soybeans (heat treatment inhibits the trypsin inhibitors)

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13
Q

Why is heat in the processing of soybeans?

A

Heat treatment inhibits the trypsin inhibitors which is important so that we can digest protein. Trypsin inhibitors would inhibit our ability to digest proteins

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14
Q

Why are peptides important?

A

Help keep calcium soluble in the small intestine which is important for absorbing the calcium

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15
Q

Casein Phosphopeptides

A

Peptides contain clutesters of serine that are phosphorylated. The multiple negative charges can interact with the calcium keeping in soluble in small intestine and available to be absorbed in the gut

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16
Q

Composition and sequence of proteins

A

Simple proteins
Conjugated proteins

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17
Q

What are simple proteins?

A

A basic polypeptide chain linked by peptide bonds

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18
Q

Example of simple proteins

A

Ovalbumin or the main egg white protein which is a water soluble protein

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19
Q

Is every simple protein water soluble?

A

Not every simple protein is water soluble so important not to assume that

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20
Q

Conjugated protein

A

Post translationally modified and may be glycosylated or phosphorylated

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21
Q

Glycosylation and example

A

glycosylated or a sugar is added to the peptide chain (good example is ovomucin another egg white protein)

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22
Q

Phosphorylated and example

A

phosphate added to peptide in the case of casein added to serene residue after translation of messenger RNA on RER

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23
Q

Protein rich sources in diet

A

Dairy

24
Q

Proteins in milk

A

Caseins and whey

25
Q

Percent of casein

A

80%

26
Q

Percent of whey

A

20%

27
Q

Percent of protein in milk

A

3.6

28
Q

Percent of protein in milk

A

3.6

29
Q

Using enzymes in cheese

A

Gives higher protein content

30
Q

Yogurt proteins

A

Use acid modification to increase protein content because proteins are coagulated by protein enzymes

31
Q

What are egg proteins regarded as?

A

High biological value (perfect protein)

32
Q

Why are eggs perfect protein?

A

Supply all the essential amino acids our bodies need for maintenance and growth

33
Q

Another complete protein?

A

Meat

34
Q

Connective tissue collagen?

A

involve in multiple levels of muscle structure helping to connect muscles to the bone (thinking about tendons)

35
Q

What does collagen contribute to?

A

Toughness

36
Q

Plant based proteins (grains and beans)

A

considered to be limiting in one or two of the essential amino acids so good to combine

37
Q

Primary structure of proteins

A

20 amino acids and sequence affects chemistry and stability

38
Q

Categories of primary acids

A

Acidic basic and hydrophobic

39
Q

Where do primary proteins structure differ?

A

All have amino and carboxylic group but the side chain (or R group) differes between they different amino acids

40
Q

Secondary protein structure

A

Alpha helix and pleated sheet with random could and beta bend

41
Q

What makes secondary structure within proteins possible?

A

Hydrogen bonds

42
Q

Alpha helix

A

spiral is stabilized at various points by hydrogen bonds
R groups make it acid, alkaline, etc
Carbonyl group involved with a hydrogen bond with an amino group of a neighbour

43
Q

Beta sheet structure

A

Multiple beta pleated sheets (first is between a and b and is parallel which comes in play from the lining up of peptides bonds and the different R groups. Amino group with amino group and each one is super impossible on the other. D and C and anti-parallel and not perfectly superimpossable on each other. We can see where there is the potential for hydrogen bonding to keep them in contact with each other and holding their structure in their native state

44
Q

Random coil

A

Random coil is how the rest of the peptide bonds can bend and coil around itself
The random coil is possible from the hydrogen bonding

45
Q

Tertiary structure

A

Intramolecular bonding and disulfide bonds and bridges

46
Q

Quaternary stucture

A

Intermolecular bonding with actin and myosin

47
Q

Biological value of proteins

A

Amino acid composition
Digestabililty

48
Q

Complete vs incomplete proteins

A

Animal vs plant

49
Q

What are some of the ways we can facilitate and enable our bodies to recover or receive nutritional value from polypeptide chains

A

Interested in digestability which involves some level of denaturation

50
Q

How to cook/ marinate proteins?

A

processing will help to denature proteins which will help with digestibility (able to access peptide links more easily)

51
Q

Digestibility

A

structure of the proteins and denaturation is going to help to unwind protein structures. Unfolding something, you can visualize/ imagine how the peptide bonds become available to proteases

52
Q

Trypsin inhibitors

A

trypsin inhibitors in soybeans and needed to deactive these in soy proteins in order to aid in protein digestibility

53
Q

Denaturation

A

Any kind of alteration to the secondary, tertiary, or quaternary structure at its most basic level
The primary structure of a protein is missing

54
Q

Heating or altering a protein

A

will be damaging and extreme
Nutritional value is then eliminated
Not part of regular food processing or cooking

55
Q

Coagulation

A

Involves taking a native original soluble protein (egg white and yolk) and expose it to heat that then transforms the previously soluble protein into a gel which is no longer water soluble

56
Q

Examples of coagulation

A

Omelette, quiche, egg bites

57
Q

What happens with heat

A

Goes from a fluid to a gel in terms of an omelet. Soluble protein (sometimes called a sol) and transforming it into a gel which is insoluble

FND 100 Final (9 decks)

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