proteins Flashcards

1
Q

proteins

A

-complex organic nitrogenous compounds made of C, H, O, N, and S
-essential
-20% of body weight
-polypeptides are made of polymerization of AA through peptide bonds
>50 aa=proteins

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2
Q

amino acids

A

composed of central C bonded to 4 groups
-amino gorup -NH2
-carboxyl group: -COOH
-Hydrogen
R group

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3
Q

essential AAs

A

9 essentials
-cant synthesize them in body
-Leucine
isoleucine
lysine
methionine
phenylalanine
threonine
valine
tryptophan
histidine

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4
Q

nonessential AA becoming essential

A

newborn, only 5 AA are non essential
metabolic pathways become more sufficient

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5
Q

protein structure

A

-primary: determine by sequence of AA (unchanged by denaturing)
-secondary: h bonding of peptide backcone
-tertiary: 3D pattern of a protein due to side chain interactions
-quat- multiple chains

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6
Q

classified by AA chains

A

dipeptide: 2
tripeptide: 3
polypeptide: more than 10
peptides: fewer than 50
proteins: more than 50

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7
Q

DandA mouth and stomach

A

Chewing in mouth (mechanical digestion)
-chemical digestion begins in stomach
-Gastrin stimulates release of HCL
-denautre proteins and activates pepsinogen to pepsin

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8
Q

DandA small intestine

A

Cholecystokinin (CCK)- peptide hormone of SI released from duodenal cells (stimulates digestion and stimulates release of pancreatic proteases)

-trypsin and chymotrypsin digest peptides to tri and di
-intestinal cells break them into amino acids
-absorbed through active transport
-transported to liver from the intestines by the hepatic portal vein

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9
Q

assimilation

A

in liver
-used to synthesize new proteins
-converted to glucose
-energy
-released to bloodstream

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10
Q

protein

A

4 cal/gram
-involved in blood clotting, fluid balance, hormone production, enzyme production, cell repair, connective tissues, neurotransmitters

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11
Q

Protein turnover

A

body constantly degrades proteins (300 pro) we only take in 65-90
-some are recycled to make new AA
-some are eliminated\
-some metabolized energy
Insulin and GH= increase protein synthesis
glucagon and cortisol= increase protein degradation

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12
Q

Deamination

A

removal of amine group
-loses an AA without transferring it to another molecule
-forms NH3
-C remanent=keto acid
-glucogenic=acid converted to glucose
ketogenic= acid to fats
-higher protein diets require more water

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13
Q

nitrogen balance

A

+N= intake is bigger than excretion
-N= intake less than excretion
zero N balance= equilibrium

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14
Q

transamination

A

forming NA AAs by transferring the N from one aa to a keto acid to form a new nonessential AA and a new keto acid

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15
Q

protein intake

A

RDA= 0.8g/kg/day
10-35%

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16
Q

digestibility

A

animal product= 90-99%
plant product= 70-90%
-soy and other legumes = >90%

17
Q

Complementary proteins

A

2 or more incomplete protein sources that in combination compensate for each other’s lack of AA

18
Q

high protein diet health effects

A

heart disease
cancer of colon, breast, kidneys, pancreas, and prostate
adult bone loss

19
Q

Kawshiorkor (protein energy malnutrition)

A

-severe protein deficiency from diet high in grains
-edema in legs, feet and stomach
-low muscle
-brittle hair-increase infection
-water and electrolyte imbalance

20
Q

Marasmus (protein energy deficiency)

A

severe deficiency in calories
-frail
-cannot stand
-older looking
-low Tb
-prone to dehydration