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Nutrition > Chapter 6: Protein > Flashcards

Chapter 6: Protein Flashcards

1
Q

Amino acid primary sequence

A

determined by the amino acid sequence

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2
Q

Polypeptide shapes- secondary structure

A

-determined by weak electrical attractions with chain
-results in twisting folding of protein
-provides strength and rigidity

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3
Q

polypeptide tangles - tertiary structure

A

-Complex structures
-due to side chain properties (hydrophillic)
-maintaining shape required to function

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4
Q

Multiple polypeptide Interactions

A
  • interactions between polypeptide chains
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5
Q

Protein denaturation

A
  • Disturbs their stability
    -uncoil and lose their shape
    -less functional ability
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6
Q

Causes of Protein Denaturation

A
  • Heat
  • Acid, Base
  • Agitation
  • Alcohol, Heavy Metals
    -other agents
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7
Q

Mouth and Salivary Glands

A

Chewing and crushing moisten protein rich foods and mix them with saliva to be swallowed

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8
Q

Stomach

A

HCl uncoils protein stands and activates stsomach enzymes

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9
Q

Small Intestine and Pancreas

A

Pancreatic and small intestinal enzymes split polypeptides further,
then the enzymes on the surface of the small intestine cells hydrolyze these peptides and the cells absorb them

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10
Q

HCl

A

Denatures protein structure
activates pepsinogen to pepsin

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11
Q

Pepsin

A

Cleaves proteins to smaller polypeptides and some free amino acids
inhibits pepsinogen synthesis

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12
Q

Enteropeptidase

A

Converts pancreatic trypsinogen to trypsin

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13
Q

Trypsin

A

-Ihnhibists trypsinogen synthesis
-cleaves peptide bonds next tothe amino acids lysine and arginine
-converts pancreatic procarboxypeptides to carboxpeptidases
-Converts pancreatic chymotrypsinogen

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14
Q

Chrymotrypsin

A

Cleaves peptide bonds next to the amino acids phonylalnine tryosine, tryptophan, methionine, asparagine and histidines

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15
Q

Protein Absorption

A

Amino acids must transport into intestinal cells
-there are specific carries for amino acids and small peptides

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16
Q

Once amino acids are in intestinal cells

A

Used for energy
synthesis of other compounds
unused proteins are sent to the liver via the bloodstream

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17
Q

Roles of Proteins

A

-Building materials for growth and maintanece
- as enzyme to help facilitate or help a reaction to completion
- As hormones messesnger molecules, released in bloodstream to tissues and elicit appropriate responses

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18
Q

Regulators of fluid balance

A

Proteins attract water
-found in blood and plasma
-do not normally cross cell membranes, when they do this causes problems for the body
-fluid balance like edema

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19
Q

Acid-Base Regulators

A

-acceot and release H+ ions to maintain balance
-disruptions may cause acidosis or alkalosis, resulting in coma or death

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20
Q

As Transporters

A

Found in nlood, cell membranes
-carrt nutrients and other molecules
-act as a pump in cell membrane

21
Q

antibodies

A

invading antigens are destroyed by antibodies
-each antigen = specific antibodies
-molecular memory is called immunity

22
Q

As a source of energy and glucose

A

Proteins can be sacrificed when needed
-body tissues broken down into amino acids
-gluconerogenesis

23
Q

Using amino acids

A

-To make other compounds
-for energy and glucose
-to make fat
- deamination reactions
creates annonia and C structure without amaino group

24
Q

Converting ammonia to urea

A

Ammonia is toxic
-the liver combines ammonia with CO2 to make urea
-Urea is released inti the blood and passes through the kidneys
-direct relationship to dietary protein intake
-water is required

25
Q

Nitrogen balance

A

nitrogen intake - nitrogen output

26
Q

Conditionally essential amino acids

A

Tyrosine becomes an essential amino acid if the body doesn’t convert phenylanine or if diet it doesn’t supply it

27
Q

Protein quality: digestibility

A

Animal protein- 90-99% soy and legume protein =less than 90%
Plant protein 70-90%

28
Q

Amino acid composition

A

Must get all 9 essential amino acids
we do not make partial proteins

29
Q

High quality proteins

A

animal derived foods and some plant derived foods

30
Q

Complementary proteins A=

A

Achieved throughout the dayas opposed to each meal

31
Q

measuring protein quality

A

0-100
100- egg whites, ground beef, chciken, skim milk, tuna

32
Q

Recommendation intakes of protein RDA

A

0.8 g/kg of healthy body weight
increased for various population groups

33
Q

DRI

A

10-35% daily intake from protein
must also ensure consumption of adequate energy daily

34
Q

reasons we need dietary protein

A

obtain essential amino acids
to supply nitrogen to make other proteins

35
Q

Protei Energy undernutrition

A

insufficient intake of protein, energy or both
most commone malnutrition
impact on children is poor growth
may impact certain adult population

36
Q

Health effects of protein

A

Heart disease
cancer
osteoporosis
weight control
kidney disease

37
Q

protein powders

A

Commonly whey protein
often used post-workout
not necessary but can be convenient

38
Q

Amino Acid supplements

A

Single amino acids do not naturally exist in food s
-possibly harmful to the body

39
Q

Difference between proteins and carbs/fats

A

Nitrogen group that is excreted as urea
they are much larger and can fold and configure themselves in unique ways
denatured proteins cannot preform functions but can’t happen to carbs/fats

40
Q

Protein synthesis

A

DNA is the templater that determines the amino acid sequence of proteins

41
Q

Translation

A

the process of mRNA directing the sequence of amino acids and synthesis of protein; the amino acids are collected by tRNA and brought to the ribosomes

42
Q

Transcription

A

the process of making mRNA from the DNA template

43
Q

Ribosomes

A

The part of the cell where translation happens and then the completed protein is released

44
Q

DNA

A

packed with 46 chromosomes
segments of DNA are genes
genes can be translated into a protein

45
Q

Gene expression

A

DNA- mRNA- tRNA -Protein
genes must be switched on and off

46
Q

single gene disorders

A

Mutations inherited at birth
damage to the individual exerted early in life

47
Q

Multigene disorders

A

Influence several genes
sensitive to interactions with the environment
single nucleotide polymorphosis

48
Q

Clinical consideration

A

-genetic predisposition to specific diseases
-personalied therapies based on genetic profile
-creation of new medicine for genetic variations
-deeper understanding of nutrition and disease pathways
-currently look mostly at SNPs

Nutrition (5 decks)

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