Chapter 7 Flashcards

1
Q

Protein

A

large, complex organic molecules made up of amino acids (contains Nitrogen)

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

Antibodies

A

Protein makes these immune molecules that tag invading organisms for destruction by the immune system

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

Major Functions of Protein

A
  • build new cells
  • component of hardened structures (hair and nails)
  • enzymes
  • lubricants
  • clotting components
  • antibodies
  • compounds that maintain pH and fluid
  • transporters
  • energy source
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

edema

A

accumulation of fluid in tissues; swelling

results from starvation

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

hair protein

A

collagen

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

nail protein

A

keratin

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

blood protein that controls fluid

A

albumin

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

pH of functioning blood and tissue fluids

A

7.35 to 7.45

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

amino acids

A

nitrogen-containing chemical units that constitute proteins

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

amino

A

portion of an amino acid that contains nitrogen

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

R group (side chain)

A

part of an amino acid that determines its physical and chemical properties

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

components of an amino acid

A

amino
R group
carboxylic acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

essential amino acids

& how many

A

amino acids the body cannot make or cannot make enough of to meet its needs (9/20)

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

nonessential amino acids

& how many

A

group of amino acids that the body can make (11/20)

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

conditionally essential

A

amino acids that are normally nonessential but become essential under certain conditions

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

precursors and derivatives of amino acids

A

precursor (amino acid used) used to make non-protein nitrogen-containing compounds

  • trytophan makes serotonin
  • tyrosine makes eoineohrine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

DNA

A

hereditary material that provides instructions for making proteins

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

gene

A

portion of DNA that codes for a protein

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

chemical attraction that connects two amino acids together

A

peptide bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

polypeptides

A

proteins comprised of 50 or more amino acids

-most naturally occurring proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

how are proteins made?

A

cells assemble 20 amino acids in specific sequence according to info from DNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

primary structure protein

A

basic structure of protein; a linear chain of amino acids linked by peptide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

secondary structure protein

A

coiling of a polypeptide chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

tertiary structure protien

A

three-dimensional, twisted structure of a polypeptide chain that includes interactions between various amino acid groups in the chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
quaternary structure protein
structure of protein that is comprised of two or more polypeptide chains arranged together in a complex manner -example: hemoglobin
26
sickle cell anemia
inherited form of anemia, abnormal blood cells that cant carry oxygen as well.
27
denaturation
altering a protein’s natural shape and function by exposing it to conditions such as heat, acids, and physical agitation
28
high-quality protein
dietary proteins that are complete and well-digested, absorbed, and used by the body
29
complete protein
dietary proteins that contain an adequate proportion of each of the nine essential amino acids
30
low-quality proteins
dietary proteins that are incomplete and have lower digestibility and bioavailability
31
imcomplete proteins
dietary proteins that contain inadequate amounts of one or more of the essential amino acids
32
limiting amino acid
essential amino acid found in the lowest concentration in an incomplete protein
33
most plant sources are not complete proteins. WHat are the exceptions?
Quinoa and soy protein
34
Where does protein digestion start?
stomach
35
Steps in Protein Digestion
HCl denatures proteins and converts pepsinogen to active pepsin, which initiates enzymatic digestion of proteins into smaller polypeptides.
36
how does the pancreas aid in protein digestion?
secretes trypsin and chymotrypsin to break down the polypeptides that enter the small intestine
37
What happens after digesting of proteins?
short peptides and amino acids are transported to absorptive cells, the peptides are broken into amino acids, which move into the capillary of the villus. travel to liver then rest of body
38
protein turnover
cellular process of breaking down proteins and recycling their amino acids
39
amino acids that are not incorporated into proteins become part of s small amino acid pool, which serves as a _______?
an endogenous (internal) source of nitrogen.
40
the human body gets how much of its amino acids from endogenous and exogenous sources.
2/3 from endogenous | 1/3 from exogenous (diet)
41
Deamination
removal of the nitrogen-containing group from an amino acid
42
what the result of deamination
the amino acid becomes a carbon skeleton
43
Transamination
transfer of the nitrogen-containing group from an unneeded amino acid to a carbon skeleton to form an amino acid
44
creatinine
nitrogen-containing waste produced by muscles
45
where do extra amino acids go if you eat too much protein?
undergo deamination, NH2 is transported to liver as glutamate, forming ammonia. liver converts ammonia to urea.
46
blood urea nitrogen (BUN)
measure of the concentration of urea in blood ( blood test that assesses kidney function)
47
Normal values fro BUN
6 to 20 mg/dl
48
urine urea nitrogen (UUN)
measure of the concentration of urea in urine - normal values 12 to 20 g in 24 hrs - measures protein intake
49
nitrogen balance (equilibrium)
balancing nitrogen intake with nitrogen losses
50
ntrogen lose comes from?
urinary elimination nail and hair grow shed the out layer of cells in intestinal tract
51
positive nitrogen balance
state in which the body retains more nitrogen than it loses - periods of rapid growth - recovering from injury or illness - weight resistance training
52
negative nitrogen balance
state in which the body loses more nitrogen than it retains - starvation - serious illness - severe injury
53
protein complementation
combining certain plant foods to provide all essential amino acids
54
protein values for average human
0.8 g/kg body weight | 10 to 35% of calories protein
55
protein-energy malnutrition (PEM)
malnutrition that occurs when the diet lacks sufficient protein and energy
56
kwashiorkor
form of undernutrition that results from consuming adequate energy and insufficient high-quality, complete protein
57
marasmic kwashiorkor
form of undernutrition that results in a child with kwashiorkor who then starts to not consume enough energy; characterized by edema and wasting
58
marasmus
form of undernutrition that results from starvation; diet lacks energy and nutrients
59
anaphylaxis
serious, life-threatening allergic reaction to food, an insect bite, a drug, or another substance such as latex
60
anaphylactic shock
an extreme drop in blood pressure
61
celiac disease
autoimmune disorder in which antibodies made against gluten react with intestinal villi; results in damage to the small intestine and poor absorption of nutrients
62
gluten
protein found in many grain-based food products
63
food provocation test (FPT)
clinical elimination-challenge test used to diagnose food intolerances
64
food intolerances
conditions characterized by unpleasant physical reactions following consumption of certain foods
65
FODMAPs
types of carbohydrates that are difficult for some people to digest and absorb -have reduced ability to absorb the frictose from bacterially digested fructan. results in bloating, gas, diarrhea.
66
phenylketonuria (PKU)
genetic metabolic disorder characterized by the inability to convert the amino acid phenylalanine into tyrosine, resulting in accumulation of phenylalanine -all infants get tested from blood at birth
67
nutritional genomics
study of nutrigenomics and nutrigenetics
68
nutrigenomics
study of how nutrients affect the expression of a person’s genome
69
nutrigenetics
study of how inherited genetic variations influence the body’s responses to specific nutrients and nutrient combinations.
70
inborn errors of metabolism
conditions that occur when genes undergo mutations that disrupt metabolism of specific nutrients (pku)