FND 100 Proteins

Question 1

What percent of caloric intake do proteins contribute to?

Answer 1

20% of total caloric intake

Question 2

How much of your plate should contain proteins?

Answer 2

1/4 of a plate serving for protein recommendations

Question 3

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

Answer 3

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

Question 4

Benefits of proteins?

Answer 4

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

Question 5

Proteins and muscles

Answer 5

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

Question 6

What are examples of structural proteins?

Answer 6

Keratin
Actin/myosin complex

Question 7

What are examples of biologically functional proteins and peptides?

Answer 7

Enzymes
Hormones
Growth factors
Trypsin inhibitor
Peptides

Question 8

What are biologically functional proteins also known as?

Answer 8

Bioactive proteins

Question 9

Examples of biologically functional proteins: enzymes

Answer 9

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

Question 10

Examples of biologically functional proteins: hormones

Question 11

Examples of biologically functional proteins: growth factors

Answer 11

Cancer cells which contain growth factors that influence cancer cell growth

Question 12

Examples of biologically functional proteins: trypsin inhibitors

Answer 12

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

Question 13

Why is heat in the processing of soybeans?

Answer 13

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

Question 14

Why are peptides important?

Answer 14

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

Question 15

Casein Phosphopeptides

Answer 15

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

Question 16

Composition and sequence of proteins

Answer 16

Simple proteins
Conjugated proteins

Question 17

What are simple proteins?

Answer 17

A basic polypeptide chain linked by peptide bonds

Question 18

Example of simple proteins

Answer 18

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

Question 19

Is every simple protein water soluble?

Answer 19

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

Question 20

Conjugated protein

Answer 20

Post translationally modified and may be glycosylated or phosphorylated

Question 21

Glycosylation and example

Answer 21

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

Question 22

Phosphorylated and example

Answer 22

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

Question 23

Protein rich sources in diet

Answer 23

Dairy

Question 24

Proteins in milk

Answer 24

Caseins and whey

Question 25

Percent of casein

Answer 25

80%

Question 26

Percent of whey

Answer 26

20%

Question 27

Percent of protein in milk

Answer 27

3.6

Question 28

Percent of protein in milk

Answer 28

3.6

Question 29

Using enzymes in cheese

Answer 29

Gives higher protein content

Question 30

Yogurt proteins

Answer 30

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

Question 31

What are egg proteins regarded as?

Answer 31

High biological value (perfect protein)

Question 32

Why are eggs perfect protein?

Answer 32

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

Question 33

Another complete protein?

Answer 33

Meat

Question 34

Connective tissue collagen?

Answer 34

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

Question 35

What does collagen contribute to?

Answer 35

Toughness

Question 36

Plant based proteins (grains and beans)

Answer 36

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

Question 37

Primary structure of proteins

Answer 37

20 amino acids and sequence affects chemistry and stability

Question 38

Categories of primary acids

Answer 38

Acidic basic and hydrophobic

Question 39

Where do primary proteins structure differ?

Answer 39

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

Question 40

Secondary protein structure

Answer 40

Alpha helix and pleated sheet with random could and beta bend

Question 41

What makes secondary structure within proteins possible?

Answer 41

Hydrogen bonds

Question 42

Alpha helix

Answer 42

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

Question 43

Beta sheet structure

Answer 43

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

Question 44

Random coil

Answer 44

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

Question 45

Tertiary structure

Answer 45

Intramolecular bonding and disulfide bonds and bridges

Question 46

Quaternary stucture

Answer 46

Intermolecular bonding with actin and myosin

Question 47

Biological value of proteins

Answer 47

Amino acid composition Digestabililty

Question 48

Complete vs incomplete proteins

Answer 48

Animal vs plant

Question 49

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

Answer 49

Interested in digestability which involves some level of denaturation

Question 50

How to cook/ marinate proteins?

Answer 50

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

Question 51

Digestibility

Answer 51

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

Question 52

Trypsin inhibitors

Answer 52

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

Question 53

Denaturation

Answer 53

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

Question 54

Heating or altering a protein

Answer 54

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

Question 55

Coagulation

Answer 55

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

Question 56

Examples of coagulation

Answer 56

Omelette, quiche, egg bites

Question 57

What happens with heat

Answer 57

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