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KIN 275 Mod 6 Proteins Pt 1

Total questions: 64

Worksheet time: 40mins

Name
Class
Date
1.

10-35% of total daily kcal (for 19+ yrs only)

a)

AMDR

b)

Animal Sources

c)

Pant Sources

d)

Proteins

e)

Dipeptide

2.

on average Canadians consume way more ______ than they need

a)

AMDR

b)

Animal Sources

c)

Pant Sources

d)

Proteins

e)

Dipeptide

3.

complete sources

a)

AMDR

b)

Animal Sources

c)

Pant Sources

d)

Proteins

e)

Dipeptide

4.

good source of B vitamins & minerals (iron, zinc, calcium)

a)

AMDR

b)

Animal Sources

c)

Pant Sources

d)

Proteins

e)

Dipeptide

5.

low in fiber - often high in saturated fat & cholesterol

a)

AMDR

b)

Animal Sources

c)

Pant Sources

d)

Proteins

e)

Dipeptide

6.

not complete sources

a)

AMDR

b)

Animal Sources

c)

Pant Sources

d)

Proteins

e)

Dipeptide

7.

Contains fiber, phytochemicals, & unsaturated fats

a)

AMDR

b)

Animal Sources

c)

Pant Sources

d)

Proteins

e)

Amino Acids

8.

chains of amino acids in different sequences

a)

AMDR

b)

Animal Sources

c)

Pant Sources

d)

Proteins

e)

Amino Acids

9.

formed by condensation & broken apart by hydrolysis

a)

AMDR

b)

Animal Sources

c)

Pant Sources

d)

Proteins

e)

Amino Acids

10.

contains between 100 - 10 000 amino acids in a sequence

a)

AMDR

b)

Animal Sources

c)

Pant Sources

d)

Proteins

e)

Amino Acids

11.

are nitrogen containing molecules that combine to form proteins

a)

AMDR

b)

Animal Sources

c)

Pant Sources

d)

Proteins

e)

Amino Acids

12.

body can break down _____ & use nitrogen

a)

AMDR

b)

Animal Sources

c)

Pant Sources

d)

Proteins

e)

Amino Acids

13.

2 amino acids

a)

Dipeptide

b)

Tripeptide

c)

Oligopeptide

d)

Polypeptides

e)

Protein

14.

3 amino acids

a)

Dipeptide

b)

Tripeptide

c)

Oligopeptide

d)

Polypeptides

e)

Protein

15.

4-9 amino acids

a)

Dipeptide

b)

Tripeptide

c)

Oligopeptide

d)

Polypeptides

e)

Protein

16.

10+ amino acids (many peptide bonds)

a)

Dipeptide

b)

Tripeptide

c)

Oligopeptide

d)

Polypeptides

e)

Protein

17.

more than 50 amino acids

a)

Dipeptide

b)

Tripeptide

c)

Oligopeptide

d)

Polypeptides

e)

Protein

18.

essential amino acids can be used to make non-essential amino acids & other (a)   compounds

19.

non essential amino acids are no less (a)   than essential amino acids

20.

can't be synthesized in the body (must be supplied by the diet)

a)

Essential Amino Acids

b)

Conditionally Essential Amino Acids

c)

Non-essential Amino Acids

d)

Amino Acids

21.

Not synthesized at a rate to meet body's needs

a)

Essential Amino Acids

b)

Conditionally Essential Amino Acids

c)

Non-essential Amino Acids

d)

Amino Acids

22.

can be synthesized in the body through transamination

a)

Essential Amino Acids

b)

Conditionally Essential Amino Acids

c)

Non-essential Amino Acids

d)

Amino Acids

23.

folds into specific orientation, giving each protein a unique 3D shape that's essential to its function

a)

Essential Amino Acids

b)

Conditionally Essential Amino Acids

c)

Non-essential Amino Acids

d)

Amino Acids

24.

linear sequence of amino acids residues

a)

Primary (1 Degree)

b)

Secondary (2 Degrees)

c)

Tertiary (3 Degrees)

d)

Quaternary (4 Degrees

25.

3D elements - alpha & beta helices, sheets

a)

Primary (1 Degree)

b)

Secondary (2 Degrees)

c)

Tertiary (3 Degrees)

d)

Quaternary (4 Degrees

26.

Further folding

a)

Primary (1 Degree)

b)

Secondary (2 Degrees)

c)

Tertiary (3 Degrees)

d)

Quaternary (4 Degrees

27.

Bonds between subunits (2 or more polypeptides interact)

a)

Primary (1 Degree)

b)

Secondary (2 Degrees)

c)

Tertiary (3 Degrees)

d)

Quaternary (4 Degrees

28.

comprise a functional protein

a)

Primary (1 Degree)

b)

Secondary (2 Degrees)

c)

Tertiary (3 Degrees)

d)

Quaternary (4 Degrees

29.

if the shape of a protein changes the (a)   changes

30.

(a)   chains fold, chains may bond together --> forms final protein

31.

almost all (a)   is digested & absorbed in small intestine

32.

proteins differ from CHO & lipids due proteins have no (a)   digestion in mouth

33.

chief cells secrete _______

a)

pepsinogen

b)

denatures

c)

pepsin

34.

Parietal cells secrete HCl that _______ protein & activates pepsin

a)

pepsinogen

b)

denatures

c)

pepsin

35.

______ cleaves peptide bonds

a)

pepsinogen

b)

denatures

c)

pepsin

36.

food allergies are triggered when a (a)   from the diet is absorbed without being completely digested

37.

people with GI disease are prone to allergies because their damaged (a)   allow for the absorption of whole proteins

38.

proteins from milk, eggs, nuts, wheat, soy, fish, shellfish & peanuts are common causes of ______ _____

(a)  

39.

a rapid, severe allergic reaction

a)

anaphylaxis

b)

Amino Acid pool

c)

amino acid

d)

Rapid turnover

e)

Slow turnover

40.

amino acids in the body tissues & fluids are collectively referred to as ___________

a)

anaphylaxis

b)

Amino Acid pool

c)

amino acid

d)

Rapid turnover

e)

Slow turnover

41.

once dietary proteins have been digested & absorbed, the ________ become available to the body

a)

anaphylaxis

b)

Amino Acid pool

c)

amino acid

d)

Rapid turnover

e)

Slow turnover

42.

insulin via increased synthesis & decreased rate of degradation

a)

anaphylaxis

b)

Amino Acid pool

c)

amino acid

d)

Rapid turnover

e)

Slow turnover

43.

collagen (structural protein)

a)

anaphylaxis

b)

Amino Acid pool

c)

amino acid

d)

Rapid turnover

e)

Slow turnover

44.

flow of amino acids through ________ is interrelated - decrease in 1 leads to increase in another

a)

anaphylaxis

b)

Amino Acid pool

c)

amino acid

d)

Rapid turnover

e)

Slow turnover

45.

Some (a)   are lost daily through shedding skin, hair, nails & intestinal cells via feces

46.

total amount of body protein is relatively (a)  

47.

new growth depends on availability of (a)   in excess of maintenance needs

48.

protein turnover rate is (a)   in pregnancy, infants, & children

49.

if limiting amino acid is _________, the body can make it

a)

non-essential

b)

essential

c)

supplied

50.

if limiting amino acid is _________, the body can break down other proteins to obtain the amino acid

a)

non-essential

b)

essential

c)

supplied

51.

if the amino acid can't be ________ then synthesis will stop

a)

non-essential

b)

essential

c)

supplied

52.

building blocks of DNA / RNA

a)

nucleotides

b)

Creatine

c)

Heme

d)

transamination

e)

deamination

53.

used for energy

a)

nucleotides

b)

Creatine

c)

Heme

d)

transamination

e)

deamination

54.

used for transporting oxygen

a)

nucleotides

b)

Creatine

c)

Heme

d)

transamination

e)

deamination

55.

used to synthesize nonessential amino acids

a)

nucleotides

b)

Creatine

c)

Heme

d)

transamination

e)

deamination

56.

is the removing of an amine group (NH2)

a)

nucleotides

b)

Creatine

c)

Heme

d)

transamination

e)

deamination

57.

produces 3C molecules that can be used to synthesize glucose

a)

nucleotides

b)

Creatine

c)

Heme

d)

transamination

e)

deamination

58.

produces 2C molecules that form acetyl-CoA for ATP production

a)

nucleotides

b)

Creatine

c)

Heme

d)

transamination

e)

deamination

59.

when protein & energy are plentiful, Amino acids undergoes _______ & used to synthesize fat for storage

a)

nucleotides

b)

Creatine

c)

Heme

d)

transamination

e)

deamination

60.

sufficient for maintenance, not sufficient for growth

a)

protein balance

b)

Positive N Balance

c)

Negative N Balance

61.

dietary N intake > N loss/excreted

Can support growth & repair

a)

protein balance

b)

Positive N Balance

c)

Negative N Balance

62.

Dietary N intake < N loss/excreted

Muscle wasting & weight loss

a)

protein balance

b)

Positive N Balance

c)

Negative N Balance

63.

(a)   act like rubber bands

64.

the fibers in tendons are constituted in large part by (a)  

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