protein Flashcards

1
Q

protein digestion in the mouth

A

protein are crushed and moistened

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

protein digestion in the stomach

A

hydrolysis of protein by hydrochorlic acid denaturation
- pepsin initiates protein digestion by cleaving proteins into small polypeptides and amino acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

protein digestion in the SM

A

pancreatic and intestinal protease hydrolyze theses further into short chains, dipeptides, and AAs
- peptidase further breaks any chains into individual AA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

protein absorption

A

specific carriers transports amino acids into cells
- once inside cells, AA can be used for energy or to synthesize compounds
- If AA are not used by the cells, they are transported to the liver

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

protein metabolism

A

-Proteins are continually being made and
broken down: turnover
-Breakdown releases AAs, forming an AA
pool
-These AAs can be used to make body
proteins or other N containing
compounds, or the C backbone can be
used for energy (gluconeogenesis)
-Turnover and nitrogen balance go hand in
hand, usually synthesis balances with
degradation, and intake from food
balances with N excretion in urine, feces, sweat

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

protein breakdown

A

-protein in your body is always breaking down and being recycled into new proteins
-the body does not store protein as it does with fat and glucose/glycogen
-AA in the pool are used, turned over stored and excreted rather fast

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

dietary protein intake

A

AMDR= 10-35%
2-3 serving
1/4 plate
RDA is 0.8/kg athletes needs 1-2g/kg

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

intake recommendation

A

-Choose lean meats and poultry and
prepare with little to no added sodium or
saturated fat
-Choose beans, peas, lentils, tofu, nuts and
seeds more often
-Choose unsweetened lower fat dairy
products
-Choose unsweetened fortified low sodium
soy beverages
*careful when judging protein intake as a
percentage of energy intake, consider the
number of grams and compare it with RDA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

who needs more protein

A

-Pregnant women
-Training athletes - leucine!!
-Growing kids
-Sick or trauma patients
-Wound healing
-Low calorie diets (15% more)
-Vegetarians (10% more)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

conditionally essential

A

Sometimes a non-essential AA becomes
essential under special circumstances
If the diet fails to supply enough or if the
body cannot make the conversion for some
reason (genetic condition, disease), then that
AA becomes conditionally essential
Phenylalanine -> tyrosine cannot happen
with PKU, so tyrosine becomes conditionally
essential

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

limiting amino acid

A

-The body can make all non-essential amino
acids given nitrogen and fragments from
carbohydrates and energy
-There are 9 amino acids that the body
cannot make either at all or in sufficient
quantities
-These must be supplied by the diet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

denaturation

A
  • secondary and tertiary structures get destroyed but primary structure is retained
    -chemical action, heat, or agitation= renders the molecule nonfunctional
    -cooking eggs and meats, digestion
    (despite the change in structure, all AA are still present = nutritionally beneficial
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Protein
Synthesis

A

The sequence of AA determines the shape
which supports a certain protein function

if you mix up the order of adding ingredients
or in copying the recipe, the product will not
turn out

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Quaternary

A

Two or more tertiary polypeptides
mixed together

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Tertiary

A

Coiled chain now all tangled up, more twists and folds resulting
from attractions or repulsions between AAs and surrounding fluids
Hydrophilic side ends up on the outer surface, and hydrophobic
groups tuck themselves inside

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

primary

A

Amino acid chain; AA put together in chain with
peptide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Secondary

A

Amino acid chain is now coiled
Determined by weak electrical attractions within the chain
These folds and twists gives proteins strength and rigidity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Acid Base Balance

A

Blood likes to be at a certain pH
Proteins have a negative charge on their surface
So they attract H+ ions to decrease acidity = acting as
buffers
They release the H+ to blood if alkaline
Extremes: acidosis or alkalosis denatures protein
rendering it nonfunctional…. ex. hemoglobin cannot
carry O2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Proteins are specific

A

If a foreign protein enters the body it is attacked
The body learns how to make antibodies (made of protein) to
attack specific protein invaders… allergies

20
Q

Essential Amino Acids

A

We have 20 AA, 9 of which are essential
These 20 AA in various combinations make all body proteins

21
Q

Conditional or Dispensable

A

The body can make these amino acids out of other amino acids
Conditional means that a certain amino acid depends on another
essential for it to be made

22
Q

protein function

A

Source of glucose = energy
Transport: lipoproteins transport across cell
membranes
Energy: 4kcal/g; goal is to not use it for energy
due to all other functions
muscle contraction

23
Q

Functions: Regulatory

A

Hormones: chemical messengers Enzymes: facilitating chemical reactions
Acid base balance Tissue & body fluid balance - proteins attract
water
Immunological: antibody synthesis

24
Q

Functions:
Structure

A

Repair
Growth
Tissue health & maintenance
Development
muscles, blood, organs, skin, hair, nails, bones

25
Q

protein energy malnutrition

A

condition that develops when diet delivers too little protein, too little energy or both. additionally many if not all of the vitamins and minerals inadequate as well

26
Q

kwashiorkor

A

protein is lacking= low albumin = edema

27
Q

marasmus

A

overall energy and nutreints lacking

28
Q

what happens if you have too much energy

A

Potentially higher intake of saturated fats and cholesterol if
intake is from animal fats = heart disease
Kidney issues due to metabolism of nitrogen
Dehydration (protein takes 7x more water to digest and
metabolize)
Lack of other nutrients

29
Q

bone health

A

high protein increase urinary excretion of calcium d/t acidity however there are a number pf beneficial effects of protein on bone health: there are no adverse effects to bone heath with high protein intake

30
Q

kidney stones

A

increased urinary excretion of calcium leads to the assumption that
kidney stones will form due to calcium build up; diets rich in protein
and low in fluid increase risk of kidney stones

31
Q

heart disease and cancer

A

concern with high protein diets is related to the nutritional
components of animal vs plant based protein - animal proteins being
higher in saturated fat, cholesterol, and lower in fiber, hence increasing
risk of heart disease. Only links with cancer to do with processed meats.

32
Q

deamination

A

Break down excess protein
by removing N and
producing ammonia and
keto acids

33
Q

keto acids

A

Used for energy, glucose,
ketones, cholesterol, fat and
carbon skeletons for non
essential AA

34
Q

non essential AA

A

Ammonia + keto; formed in liver. Ammonia is toxic,
combines with CO2 to make
urea

35
Q

250 g

A

Max rate of metabolism of
ammonia by the liver

36
Q

too much PRO

A

if we have too much protein,
the body cannot metabolize
all the ammonia

37
Q

Urea

A

Urea goes to blood then to
kidneys for filtering to make
urine

38
Q

water

A

Need water to excrete urea =
dehydration = weight loss

39
Q

liver/kidney

A

liver disease = blood NH3
kidney disease = blood urea high

40
Q

protein quality

A

Digestibility: depends on protein
source and other foods eaten with it
(plant vs animal proteins)
Amino acid composition - foods need
to provide the essential amino acids,
and those that are conditionally
essential for some
The body makes whole proteins ONLY,
if one AA is missing, the protein will
not be made

41
Q

animal protein foods

A

Easiest to digest and absorb
(90%)
All sources have all essential AA
Complete proteins
Absorption of any protein
improves if eaten with CHO
and/or fats

42
Q

plant protein foods

A

Legumes are next best (80%)
Other plant sources range from
60-90%
Do not contain all essential AA
in sufficient amounts, therefore
are incomplete proteins
Must complement protein
sources to get all AA… combine 2
grains, legumes, nuts, seeds
Need 10% more protein because
of poorer absorption and quality

43
Q

why do vegatarian need more pro

A

plant base proteins are incomplete protein therefore you need to eat more to receive all the essential amino acids

44
Q

pros of veg

A

Higher fiber intake
Higher intake of healthy fats
Cost effective
Lower in saturated fat
Grains, fruits, veg, nuts, seeds are nutrient
dense

45
Q

cons of veg

A

Iron, Calcium, B12, Zinc, Omega 3s found
in highest quantities in animal foods
Potentially not fortified
Risks of missing essential AA
Need to know complimentary proteins