Chapter 8 Flashcards

Proteins and alcohol (55 cards)

1
Q

what parts make up the structure of protein?

A

-central carbon
-nitrogen
-carboxylic acid
-side chain

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2
Q

what does the side chain of an amino acid provide?

A

unique chemical function

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3
Q

what are the 9 essential amino acids?

A

isoleucine, leucine, valine, phenylalanine, tyrptophan, histonine, lysine, threonine, methionine

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4
Q

what are the 12 nonessential amino acids?

A

alanine, glycine, proline, tryrosine, aspartic acid, glutamic acid, arginine, serine, cysteine, asparagine, glutamine

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5
Q

what are the 4 protein structures?

A

-primary (simple amino acid chain)
-secondary (ribbon)
tertiary (some proteins end here)
quaternary (4 tertiary groups together)

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6
Q

what causes proteins to denature?

A

Heat, pH, enzymes

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7
Q

how are proteins made?

A

-proteins are made by linking amino acids through peptide bonds
-DNA-> RNA-> Protein

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8
Q

1st step in making proteins

A
  1. the DNA unwinds from its super-coiled state
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9
Q

2nd step in making proteins

A
  1. unwinding allows the DNA code for the amino acid sequence to be transcribed into complementary messenger RNA (mRNA) labled as primary RNA transcript)
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10
Q

3rd step in making proteins

A

the DNA stays in the nucleus and the mRNA travels in the cytosol

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11
Q

4th step in making proteins

A

the ribosomes read the codons on the mRNA and translate the instructions to produce a specific protein.
-A protein synthesis begins at a specific starting point, indicated by ALUG. the initiation complex forms when the ribosomla subunits and the first tRNA molecule locks into a stand of mRNA
-B. trnasfer RNA (tRNA) units bring amino acids to the ribosomes as neeeded dduring prtoein synthesis. The tRNA carriers have a compementary code to the mRNA- such that, if the amino acid arginine is needed during synthesis, the AGA on the mRNA would corresponf to UCU on the tRNA . Numerous tRNA carriers are present during prtoen synthesis to continually supplu the ribosomes with needed amino acids. ATP is used to supply the energy needed to activiate the tRNA in order to form each new peptide bond
-C. protein synthesis continues by adding 1 amino aicid at a time to the growing polypeptide chain until a specific ending (stop) codon is reached or when a needed amino aicd is not available
-D. the polypeptide is then released from the ribosome when it encounters the ending (stop) codon

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12
Q

what causes sickle cell anemia?

A

a mutation occurs on the T-A
-causes clumped hemoglobin
-blood cells stick together and are irregularly-shaped

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13
Q

what are essential amino acids?

A

-they cannot be synthesized
-conditionally essential amino aicd that is essential because the individual lacks the enzymes to synthesize the normally nonessential amino acid (phenylalanine hydrolase)

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14
Q

what is transamination?

A

process for synthesizing nonessential amino acids
-“carbon skeleton” from a metabolic cycle accepts amino group to become amino acid
-available for protein synthesis
-Vitamin B6 is required for transamination

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15
Q

what is Deamination?

A

-amino group is incorporated into urea for excretion
-alpha keto acids can be used for energy, or as substrates in krebs cycle

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16
Q

what are complete protiens?

A

high levels of all essential amino acids
-animal protein (not geletin)
-quinoa, soy
-complimentary proteins

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17
Q

what are incomplete proteins?

A

-deficient in at least 1 essential amino acid
-plant proteins

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18
Q

what is biological value (BV)?

A

-ratio of nitrogen retained to nitrogen absorbed
-N retained/N absorbed
-measures how efficently the absorbed food protein can be turned into body tissue
how close is the food’s AA pattern to that of body tissues

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19
Q

what is the protein efficiency ratio (PER)?

A

-FDA uses for labeling regulations for infant food
-compares the weight gained in a growing rat after 10 days or more eating a standard amound of a specific protein source
-(g weight gain/g protein consumed)

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20
Q

what is chemical score?

A

-(mg of limiting amino acid/gram of protein)/ (mg f limiting amino acid/gram of ideal protein)

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21
Q

what is the Protein Digestibility Corrected amino acid score (PDCAAS)?

A

-PDCAAS=chemical score
-*digestibility score

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22
Q

nitrogen balance

A

-meathod to determine protein needs

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23
Q

healthy people replace protein lost

A

-not recovering from injury of illness
-not growing

24
Q

negative nitrogen balance

A

intake<losses
elderly, caloric deficit, sick, injured, recovering from surgery

25
positive nitrogen balance
intake>losses babies, pregnant women, body builders
26
Measuring Nitrogen Balance
N intake from diet vs. N loss from body Measuring N intake: protein is 16% N.-N (g) x 6.25= protein (g) estimating N loss: NB= protein intake- g urinary urea N- (0.2 x urinary urea N)- 2g (from other body sources; hair, skin, feces)
27
Protein RDA
-0.8 g protein/ kg healthy BW/day (56 for 70 kg man) -increased 25 g/d 2nd and 3rd trimester of preg. lact. AMDR: 10-35% of kcal
28
American consumption
-Men about 100 g/d -women 65 g/d -15.2%
29
what happens to excess protein
-not stored -N excreted -C skeletons used for energy
30
protein digestion
-protein break down begins with cooking -stomach acid denatures protein -pepsin breaks hydrolyzes protein into peptide fragments -in duodenum chymotrypsin, trypsin, and carboxypeptidase are released by pancreas (cleave peptides from stomach into smaller fragments) -enzymes at the brush boarder and in the enterocytes cleave di and tripeptides in to individual amino acids
31
protein digestion in stomach
protein is partially digested by the enzyme pepsin and hydrochloric acid
32
pancreas digestion in pancreas
further protein digestion by enzymes released by the pancreas into the small intestine
33
digestion in small intestine
final digestion of protein to amino acids occurs in the small intestine
34
digestion in liver
amino acids are absorbed into the portal vein and transported to the liver. from there they enter the general bloodstream
35
digestion in large intestine
little dietary protein is present in feces
36
what are the functions of protein in the body?
-energy -glucose formation -acid-base balance -structure -immune function -protein hormones and enzymes -fluid balance
37
energy function
-5-10% of enegy used in body (expensive energy) -prolonged exercise (increases 10-15%- branched chain AA in. muscle-Leucine, isoleucine, valine) -if there are insufficient total calories, then dietary (and body) protein is used for energy
38
glucose formation function
-gluconeogenesis for brain and RBC between meals and low CHO diets
39
acid-base balance function
regualtion of pH by buffering resulting from charged amino acid side chains
40
structure function
-connective tissue, bone matric, epidermal cell walls (skin), lipoproteins, antibodies, etc -collagen, actin and myosin, plus hemoglobin make up 50% of the protien in the body
41
immune function
immune cells require protein
42
protein hormones and enzymes function
-insulin, pituitary hormones, thyroid hormone -enzymes for thousands of metabolic reactions
43
what is swollen tissue (edema)
-nutrition related:insufficient protein -low albumin in blood -excess fluid interstitial place -leads to edema
44
hydrostatic pressure
blood pressure forces fluid and nutrients into cells
45
osmotic pressure
albumin and globulins attract fluid back into blood
46
althetes protein intake
-1.2 g/kg/day for endurance athletes -1.6-1.8 g/kg/day for resistance training
47
Kwashiorkor
-severe protein defecit (with moderate energy) -edema -weight loss -mainteneace of some muscle and fat -growth impairment rapid onset -fatty liver
48
marasmus
-severe weight loss -wasting of muscle and body fat -severe growth impairment -develops gradually
49
excess protein (NAS)
-45% kcal from protein- weakness, nausea, diarrhea, death ("rabbit starvation") -maximum rate of urea synthesis/excretion at 250 g protein/day (approx 40% kcal) -high protein does not prevent loss of lean tissue during calory defecit
50
fate of amino acids in AA pool
input: internal turnover, dietary sources major uses: fat, glucose, energy, protein synthesis deamination, kidney disposal of NH3
51
glucogenic amino acids
glycine serine caline histidine arginine cytesine proline hydroxyproline alanine glutamate aspartate asparagine methionine
52
ketogenic amino acids
leucine and lycine -> give rise to acetyl CoA -> used in TCA cycle
53
both ketogenic and glucogenic amino acids
threonine isoleucine phenylaline tyosine tryptophan
54
possible advantages of vegetarianism
-lower rates of some chronic disease (CDH, hypertension, type II diabetes, obesity, some cancers) -
55
possible disadvantages of vegetarianism
-nutritent deficiencies if uninformed- B12, Fe, Zn -deficinecies and growth retardation in children of uninformed vegetarian parents -less nutrient-dense sources of lysine, methionine, vitamins B12, D, Ca, Fe, Zn, riboflavin