Module 8 Flashcards

1
Q

What are the three main amino acid groups?

A
  • Nitrogen containing amine group
  • Carboxylic acid
  • A side chain
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2
Q

How many amino acids are there?

A

21

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3
Q

What is a complete protein?

A

Foods with nine essential amino acids

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4
Q

What are sources of complete protein and in-compete protein

A
  • Complete = animal
  • Incomplete = plant
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5
Q

The amino acid that is lacking is called..

A

Limiting amino acid

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6
Q

What are the steps for protein synthesis

A
  1. RNA makes a copy of the DNA code for a particular gene
  2. The RNA message has a code that controls the sequence of amino acid needed to build the specific protein. These amino acids are drawn from the amino acid pool
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7
Q

How do primary structures arise

A
  • Arise from adjacent amino acids bonding to each other
  • Occurs through condensation reaction and leads to formation of a peptide bond
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8
Q

What does peptide bonds lead to

A
  • Polypeptide
  • Not yet a protein it must fold into secondary, tertiary or perhaps quaternary structure
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9
Q

How do secondary structures arise

A
  • Hydrogen bonds between non-adjacent amino acids
  • Formation of alpha helices and beta-pleated sheets
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10
Q

How do tertiary structures arise

A
  • Interactions between amino acids side chains
  • Formation of polypeptide chain
  • Might result in functional protein
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11
Q

What are quaternary structures

A
  • Several proteins with a tertiary structure to form a final protein
  • Called a protein subunit
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12
Q

What happens when a protein denatures

A
  • Loses its folded 3D structure
  • Loses its function
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13
Q

What causes denature of protein

A
  • Acid in our stomach, heat, agitation
  • Once denatured it cannot be reversed
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14
Q

Describe the protein digestion process

A
  1. Mouth: no chemical digestion, only mechanical
  2. Stomach: HCL denatures proteins; pepsin chemically digests protein
  3. Pancreas: secretes pancreatic proteases, including chymotrysin and trypsin
  4. Small intestine: majority of protein digestion; pancreatic proteases chemically digest protein
  5. Large intestine: minimal protein digestion
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15
Q

What are the functions for protein

A
  • Body structure
  • Transport
  • Enzymes
  • Movement
  • Fluid balance
  • Protection from disease
  • Energy
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16
Q

What is the protein body structure

A
  • Bones, muscles, skin and every body organ contain protein
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17
Q

What is the main structural protein

A

Collagen

18
Q

What is the other key structural protein

A

Elastin, permits elasticity

19
Q

Function of transport in protein

A
  • Protein tracks in cells allow substances to walk along them, permitting transport around the cell
  • Protein channels regulate movement into and out of the cell
20
Q

What is the blood protein and what does it do

A
  • Hemoglobin
  • Transports oxygen around the body
21
Q

Function of enzymes in protein

A
  • Most enzymes are proteins
  • Speed up rate of reactions
22
Q

Function of movement in protein

A
  • Myosin and actin are found in muscle
  • When myosin proteins attach to actin and kink their heads, muscle contraction occurs
  • Allow our bodies to produce movement
23
Q

Function of fluid balance in protein

A
  • Water is attracted to positive and negative charges of amino acids in blood proteins
  • This draw water into the blood and out of the extracellular space
  • If blood proteins are low, fluid can build up in the extracellular space leading to edema
24
Q

Protein protection from disease

A
  • Collagen in skin helps restrict what can enter body
  • If infectious agents enter, Y-shaped proteins called antibodies stick to these agents, promoting their removal and limiting the harm they can cause
25
Q

What is the first line of defence and second line

A
  • First line, collagen in skin
  • Second line, antibodies
26
Q

Function of energy in protein

A
  • Proteins provide 4 kcal/gram
  • Amino acids for energy is a wasteful process
  • Body prefers to use protein for its various other functions
27
Q

Synthesis of non-protein substances

A
  • Creatine, DNA, RNA, dopamine and serotonin
28
Q

What is marasmus

A
  • Occurs when energy and protein are deficient
  • Promotes anemia, dehydration, heart irregularities, body temperate dysregulation
29
Q

What is kwashiorkor

A
  • Believed to occur when protein is deficient, but energy is sufficient
  • Evidenced by a distended, swollen abdomen and an otherwise slim appearance
30
Q

How can protein promote caloric deficit

A
  • Promoting fullness
  • Contributing to carbohydrate and lipid metabolism
  • Requiring more energy to digest and absorb it
31
Q

Protein and muscle growth

A
  • Protein muscle synthesis increases in the 24 hours following weight training
  • 10g of essential amino acids in the first 2 hours following exercise encourages muscle growth
  • Milk-based proteins, for instance, increases muscle strength and improves body composition
32
Q

Protein and bone health

A
  • In bone, collagen forms a matrix that minerals (ex. Calcium) harden
  • However, high protein diets can promote calcium excretion
  • Overall, high protein diets do not seem to negatively affect bone health
33
Q

Protein and kidney health

A
  • High protein diets tax the kidneys because they have more waste products to excrete
  • For those with reduced kidney function, consuming protein at the recommended intake level (0.8 g/kg), and not beyond it, is recommended
34
Q

Protein quality factors

A
  • How well a protein is digested
  • How the types and quantities of amino acids in that protein source match the body’s requirements.
35
Q

What is the PDCAAS

A
  • Compares the amino acid content of a food against a standard amino acid profile. The highest score that can be achieved is 1.0
36
Q

What is the DIAAS

A
  • Measures how well amino acids are digested in the ileum and more closely estimates the amount of amino acids absorbed by the body
37
Q

What is the PER

A
  • How much weight an animal gains when consuming a specific amount of protein, divided by the amount of food it consumed
38
Q

What are branched-chain amino acids

A
  • essential amino acids that have a branched side chain
  • They account for 35-40% of the dietary essential amino acids found in body protein
  • Have been shown to reduce muscle damage associated with weight training
  • Can be consumed from whole sources, do not have to come from supplements
39
Q

Animal source of protein

A
  • Animal proteins have more total protein, a higher PDCAAS and are complete proteins
  • Also, they have vitamin B12 and are higher in vitamin D, iron, zinc and omega-3 fatty acids
  • However, they are also higher in saturated fat and are absent in fibre, phytochemicals
  • Also, processed animal products (ex. Deli meats, bacon) increase CVD risk/mortality
40
Q

Risk of vegetarian diets

A
  • They are lower in vitamin D, omega-3 fatty acids, calcium, iron and zinc
  • Vitamin B12 is only found in animal products (with the exception of nutritional yeast)
  • Supplementation is recommended if these are not sufficient in diet
41
Q

Benefits of vegetarian diets

A
  • Diets are high in fibre and phytochemicals and low in saturated fats
  • Vegetarians are more likely to have lower BMIs, total cholesterol and LDL
  • They are also at lower risk for heart disease, cancer and CVD mortality