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Certified Nutrition Coach > Ch 6: Protein > Flashcards

Ch 6: Protein Flashcards

1
Q

Products of Protein

A

Muscles, bones, hormones, neurotransmitters

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2
Q

Process of communication between cells by biological messengers to govern cellular function

A

Cell Signaling

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3
Q

Chemical structures containing only carbon, hydrogen, oxygen, and/or nitrogen.

A

Organic Molecule

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4
Q

The organic building blocks of proteins containing both a carboxyl and an amino group.

A

Amino acids

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5
Q

Second-most abundant molecule in fat-free bodily tissues (water being the most abundant)

A

Protein

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6
Q

How many Amino Acids are there?

A

20

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7
Q

Five components of Amino Acids

A
  1. Central Carbon
  2. Carboxyl Group (Organic Acid -COOH)
  3. Hydrogen
  4. Amino Group (NH2)
  5. Side Group (R Group)
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8
Q

What makes an Amino Acid unique

A

Its Side Group

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9
Q

Types of Amino Acids

A

Essential, Conditionally Essential and Nonessential

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10
Q

Type of Amino Acid that must be consumed in the diet because they are necessary for bodily function and cannot be synthesized by the body

A

Essential Amino Acids
There are 9 including 3 Branched

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11
Q

Considered nonessential under normal circumstances and can be synthesized in the body; however, under certain physiological conditions, requirements can outweigh their availability or rate of synthesis, making them essential for some individuals

A

Conditionally Essential Amino Acids
There are 6

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12
Q

Instances for Conditional Amino Acids

A

Infancy, Injury, Disease or Trauma

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13
Q

Amino Acids Synthesized by the body

A

Nonessential Amino Acids
There are 5

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14
Q

The Essential Amino Acids

A

PVT TIM HALL
P - Phenylalanine
V - Valine
T - Threonine
T - Tryptophan
I - Isoleucine
M - Methionine
H - Histidine
A - Arginine*
L - Lysine
L - Leucine

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15
Q

Branched Amino Acids

A

Isoleucine

Leucine

Valine

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16
Q

Nonessential Amino Acids

A

Alanine

Asparagine

Aspartic acid

Glutamic acid

Serine

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17
Q

Conditionally Essential Amino Acids

A

Arginine

Cysteine

Glutamine

Glycine

Proline

Tyrosine

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18
Q

May become acetoacetate (a ketone body) or acetyl-CoA prior to entering the Krebs cycle for the generation of ATP

A

Ketogenic Amino Acids

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19
Q

Ketogenic Amino Acids

A

Leucine

Lysine

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20
Q

Amino Acids that have the potential to become glucose for use in energy metabolism

A

Glucogenic Amino Acids

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21
Q

Glucogenic Amino Acids

A

Alanine

Asparagine

Aspartic acid

Cysteine

Valine

Glutamic acid

Glutamine

Glycine

Proline

Serine

Arginine

Histidine

Methionine

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22
Q

Ketogenic or Glucogenic Amino Acids

A

Tyrosine

Isoleucine

Tryptophan

Phenylalanine

Threonine

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23
Q

Products of Protein Synthesis (Process of joining amino acids with peptide bonds to form proteins.)

A

Collagen, Myosin, Hemoglobin

24
Q

The joining of two large molecules by removing one hydrogen from one molecule and a hydroxyl group (OH) from another molecule and then binding the two larger molecules together on the newly freed bonds.

A

Dehydration Synthesis

25
Q

The bond between two amino acids, occurring between the carboxyl group of one and the amino group of the other.

A

Peptide Bond

26
Q

Breakdown of one large molecule into two smaller molecules via the donation of one hydrogen and one hydroxyl group from water to the smaller molecules, respectively.

A

Hydrolysis

27
Q

Two Peptides are joined
Three Peptides are joined
Four or more peptides are joined
10 or more peptides joined

A
  • Dipeptide
  • Tripeptide
  • Oligopeptide
  • Polypeptide
28
Q

Bodily peptides are typically at least how many peptides

A

50 or more

29
Q

Three major muscle proteins

A

Actin , Myosin (Uses ATP to grab Actin) and Titin (Elasticity)

30
Q

Process of changing a protein’s shape, but not its primary structure

A

Denaturation

31
Q

First step in Protein breakdown

A

Denaturation (temperature, pH, and enzymes)

32
Q

Process of Protein breakdown

A

Chewing releases Gastrin (Hormone that release digestive fluids) from stomach, which causes release of Hydrochloric Acid (HCl) which releases Pepsin (Enzyme that breaks down peptide bonds in a Hydrolysis reaction). The smaller peptide chains move to the Small Intestine

33
Q

Peptide chains to the Duodenum

A

Intestinal cells release Secretin (regulator of digestion–reduced pH) and Cholecystokinin (acts on pancreas to release the Proteases Enzymes: Trypsin, Chymotrypsin, Carboxylpeptidase and Elastase

34
Q

reduce the size to single amino acids and dipeptides, which can then be absorbed from the small intestine into the hepatic portal vein, carrying them to the liver.

A

Peptidases and aminopeptidases

35
Q

Amino Acids in the Liver

A

Amino acids may be used for protein synthesis, broken down into urea (urine waste), converted to carbohydrate or fat (gluconeogenesis or ketogenesis), metabolized for energy, or released into the peripheral blood stream for use throughout the body.

36
Q

Protein Function

A

Protein and amino acids are primarily used to create bodily tissues; to form enzymes and cellular transporters, as cell signals; to maintain fluid balance; to buffer acids and bases (pH balance), in the production of hormones and neurotransmitters; and in the immune system.

37
Q

Bones are made of?

A

Calcium and Collagen (also skin, tendons, ligaments, and joints)

38
Q

Collagen composition

A

glycine, proline, and hydroxyproline

39
Q

Protein found on the cell membrane that transports sodium and potassium to create an electrochemical gradient across the membrane

A

Sodium-Potassium Pump
Potassium into the Cell
Sodium out of the cell

40
Q

Enzyme involved in the metabolism of glucose

A

Pyruvate dehydrogenase (converts the end product of anaerobic glycolysis, pyruvate, to acetyl-CoA for use in the Krebs cycle within the mitochondria)

41
Q

Increase in the amino acid leucine

A

Signal muscle cells to begin synthesizing new proteins when the other necessary amino acids are present

42
Q

Proteins and pH balance

A

Proteins and amino acids help regulate the body’s acid–base balance by binding to free hydroxyl groups or hydrogen ions in the blood to help maintain a neutral pH (Hemoglobin) prevents CO2 from forming Carbonic Acid

43
Q

Peptide Hormones

A

Human Growth Hormone, Insulin, gastrin and leptin

44
Q

Daily protein requirement

A

85 - 95 grams of protein per 2000 calories, 17 - 18% of total calories

45
Q

Established by the Food and Nutrition Board of the Institute of Medicine, They establish the recommended dietary allowance (RDA) for protein, last revised in 2005

A

Dietary Reference Intake (DRI)

46
Q

Dietary Reference Intake (DRI) for protein

A

46 grams per day for women, 56 grams for men
Based on 0.8 grams of protein per kilogram of body weight per day

47
Q

Amount of nutrient needed to meet the needs of almost all individuals in an age–sex group.

A

Recommended Daily Allowance (RDA)

48
Q

Factors for Daily Protein Requirement

A

Body size, activity level or sport, and body composition goals of the individual

49
Q

Total Daily Protein Requirements average person

A

0.8 - 2.2 grams per kilogram

50
Q

Quality of the amino acids found in, and the digestibility of, a protein

A

Protein Quality

51
Q

A protein that contains sufficient quantities of all essential amino acids.

A

Complete Protein (animal products and Soy)

52
Q

Two incomplete proteins that, when consumed together, mimic a complete protein by providing all essential amino acids.

A

Complementary Protein

53
Q

Rice Proteins

A

Rice proteins are poor sources of lysine, but they are rich in cysteine and methionine

54
Q

Bean Proteins

A

Beans have enough lysine, but they are poor sources of methionine and cysteine.

55
Q

Examples of Complementary Proteins

A

wheat/peanut butter, pasta/peas, and lentils/almonds

56
Q

Primary factor for increasing muscle protein synthesis to facilitate muscle recovery and growth

A

Leucine
Leucine is capable of enhancing muscle protein synthesis signaling for a period of about 3 hours after ingestion, and the optimal dose to maximize protein synthesis is 0.05 grams of leucine per kilogram of body weight

57
Q

Protein timing

A

Therefore, 24-hour net muscle protein synthesis may be optimal if stimulated with dietary protein (containing leucine) every 3 hours
every meal should contain at least 0.4 grams of protein per kilogram of body weight and at least four meals should be consumed throughout the day

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