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NUFS 108A > Protein - Exam 3 > Flashcards

Protein - Exam 3 Flashcards

1
Q

Protein Distinguishers

A

Body Protein, Dietary Protein, Enzymes

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2
Q

Location of 40% of body protein

A

Skeletal Muscles

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3
Q

% of protein in body organs

A

~25%

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4
Q

Amino Acids Elements

A

H, O, C, N

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5
Q

Amino Acid Functional groups

A

Amino group, Carbon Skeleton, Acid (carboxyl group), R group (side chain)

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6
Q

Peptide Bond Formation

A

Condensation Reactions (release water)

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7
Q

Sulfur Containing Amino Acids

A

Cysteine (C) & Methionine (M)

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8
Q

Aromatic Ring Containing AAs

A

Phenylalanine (F), Tryptophan (W), Tyrosine (Y)

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9
Q

Branched-Chains Amino Acids

A

Leucine (L), Isoleucine (I), Valine (V)

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10
Q

Net Charge AA Classifications

A

Negatively Charge, Positively Charge, Neutral (no charge)

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11
Q

Negatively Charged AAs

A

Aspartic Acid (D), Glutamic Acid (E)

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12
Q

Positively Charged AAs

A

Arginine (R), Histidine (H), Lysine (K)

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13
Q

Polarity of AAs

A

Wether it likes aqueous or fatty environments

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14
Q

Polarity options of AAs

A

Polar Neutral AAs, Polar charged AAs, Nonpolar neutral AAs, Relatively Nonpolar AAs

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15
Q

Classification of AAs

A

Structure, Net charge, Polarity, Essentiality

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16
Q

Conditionally Indispensable AAs

A

Have Precursors - Can’t always synthesize them under certain life stages or situations

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17
Q

Protein Digestion Begins…

A

In the Stomach

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18
Q

After absorption, which organ takes up most dietary amino acids

A

The liver

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19
Q

First step of AA catabolism

A

Removal of amino group via transamination or deamination

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20
Q

Transamination Importance

A

Important for synthesis of many dispensable (non-essential) AAs

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21
Q

ALT & AST transamination biomarker importance

A

Markers of liver (necrosis) issues
AST more sensitive to liver, ALT more SPECIFIC to liver

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22
Q

What is the alpha-keto acid of alanine?

A

Pyruvate

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23
Q

What is the alpha-keto acid of glutamate?

A

a-ketoglutarate

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24
Q

What products are generated in deamination reactions?

A

Ammonia and alpha-keto acid

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25
Q

How are the urea and TCA cycles connected?

A

CO2 (TCA to urea) provides Carbon, fumarate (urea to TCA), oxaloacetate (TCA to Urea) aspartate provide N

26
Q

structure of urea

A

One N from ammonia (oxidative deamination), one N from aspartate in urea cycle, C from CO2, O2 from water

27
Q

Where in the cell does the urea cycle take place?

A

Mitochondria (step 1 & 2) & cytoplasm (step 3, 4 & 5)

28
Q

In which organs/tissues does the urea cycle occur?

A

Urea cycle = Liver (organ) /Hepatocytes (tissue); ***then travels in blood to kidneys for urine production

29
Q

What are all the possible fates of amino acids upon catabolism?

A

Amino groups = ammonia (5% excreted in intestinal tract) - urea (95% excreted in kidneys)
Carbon Skeleton = Energy (TCA cycle), Glucose (TCA cycle & gluconeogenesis), Ketone Bodies, Lipids

30
Q

What’s the difference between glucogenic and ketogenic amino acids?

A

Glucogenic = can be used to make glucose
Ketogenic = must generate acetyl-CoA or acetoacetate to create ketone bodies

31
Q

Common Transamination

A

producing glutamine from alanine (dependant on Vit B-6)

32
Q

Most common deamination

A

deamination of glutamate (more when we have a low energy state in the cell) ***a-ketoglutarate can enter TCA cycle to produce energy

33
Q

After absorption, which organ takes up most dietary amino acids?

A

THE LIVER - main site of catabolism of indispensable (essential) AAs *exception to BCAAS (tend to be utilized by muscles/heart)

34
Q

PKU, phenylketonuria

A

Genetic Condition - “inborn error of metabolism” -Phenylalanine hydroxylase exhibits little to no activity &
Tyrosine becomes essential

35
Q

Outcome of PKU

A

Phenylalanine accumulates in the brain & can cause psychological issues (thinking, concentration & morbidity if not controlled)

36
Q

How is protein quality determined?

A

Amount of essential AAs, digestibility & bioavailability

37
Q

Complete Protein

A

sufficient amount of essential amino acids (all 9), with optimal digestibility & bioavailability

38
Q

Complete Protein options

A

Dairy, eggs, meat, fish, poultry (exception:gelatin lacks Trp)

39
Q

Incomplete Protein

A

-Limiting amino acid, main one…sometimes more. Often have to have with mutual supplementation or complementary foods

40
Q

Incomplete protein options

A

Legumes, nuts, seeds, vegetables, grains/cereals (exception: soy, quinoa, chia seeds)

41
Q

Protein RDA

A

RDA = 0.8g pro/kg body weight
*focused on nutrient specific recommendations

42
Q

Protein AMDR

A

10-35% of energy intake *focused on dietary pattern (large goal)

43
Q

Amino Acid (Protein Functions)

A

Catalysts, Messengers (hormones), Structural elements (actin, myosin), Buffers, Fluid balancers (plasma proteins-oncotic pressure), Immunoprotectors (antibodies, immunoglobulins), transporters

44
Q

Amino Acid non-energy metabolism functions

A

Synthesis of: Nonessential AAs, proteins/enzymes, n-containing nonprotein compounds, neurotransmitters, neuropeptides, hormones

45
Q

Nitrogen Containing Nonprotein Compounds

A

Carnitine, Creatine, Choline, Pyrimidine/Purine

46
Q

What is carnitine

A

N-containing compound made from lysine in the liver and found in food (beef,pork)

47
Q

Why is carnitine important

A

(1) needed for transport of LCFAs across the inner mitochondrial membrane
(2) Needed for ketone catabolism for energy
*adequate lysine makes enough carnitine for fat burning

48
Q

Use of Creatinine in clinical setting

A

cyclized creatine - used as a biomarker of existing muscle mass/kidney function in the urine or blood

49
Q

What is Creatinine

A

Cyclized creatine

50
Q

What is creatine

A

N-containing non-protein compound (ergogenic aid) found in meat, fish, or synthesized from AAs in kidneys/liver (de novo)

51
Q

Functions of choline

A

Structural functions, blood clotting functions, signaling functions, methyl donor function

52
Q

Foods containing choline

A

eggs, meats, organ meats, shrimp, cod, salmon, wheat germ, legumes

53
Q

Functions of choline (longer)

A

Synthesis of phosphatidylcholine and sphingomyelin in the body, forms platelet aggregating factor and the neurotransmitter acetylcholine, oxidation to form betaine with roles in methionine and folate metabolism

54
Q

What are pyrimidines and purines?

A

Building blocks or RNA/DNA - nitrogen containing rings
-Purines (adenine and guanine) are two-carbon nitrogen ring bases while pyrimidines (cytosine and thymine) are one-carbon nitrogen ring bases.

55
Q

4 levels of protein structure

A

Primary - Sequence of AAs
Secondary - hydrogen bonding = a-helix & b-sheets
Tertiary - further folding of peptide chains (side chain interactions)
Quaternary - protein made of 2 or more peptide chains

56
Q

Why is protein turnover constant?

A

Because it is not stored - to synthesize new protein usually need to recycle AAs from other sources… which causes constant turnover

57
Q

ubiquitination

A

adding ubiquinones onto the peptide (tags), once tags it’s sensed by protein complex to start degrading back into the AA pool

58
Q

Energy expenditure of protein turnover

A

10-25% resting energy expenditure

59
Q

Positive nitrogen balance

A

(growth) - more protein synthesis
-childhood/pregnancy/muscle mass (weight training)/weight gain as adult

60
Q

Negative nitrogen balance

A

(injury/illness) more protein degradation
-actively loosing weight

61
Q

nitrogen balance state

A

“Typical healthy adult” N-in=N-out…. *never truly in a balance. Typically assessed in 24hour time period

NUFS 108A (3 decks)

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