LESSON 10: PROTEINS Flashcards

1
Q

A compounds of CARBON, HYDROGEN, OXYGEN AND NITROGEN arranged into amino acids linked in a chain; 20 different amino acids,

A

PROTEINS

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2
Q

Has the same basic structure: a central carbon atom with a hydrogen (H) group, an amino group (NH2), and an acid group (COOH) attached to it

A

AMINO ACID

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3
Q

3 According to Essentiality

A
  • ESSENTIAL AA
  • SEMI-ESSENTIAL AA
  • NONESSENTIAL AA
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4
Q

That the body cannot make at all or cannot make in sufficient quantity to meet its needs

Ex: Isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine

A

essential aa

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5
Q

Are those whose rate of synthesis in the body is inadequate to support growth and are therefore needed by young animals

Ex: Arginine, histidine

A

SEMI-ESSENTIAL

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6
Q

Can be synthesized in the body in sufficient amounts

EX: Alanine, asparagine, aspartic acid, cystine, cysteine, glutamic acid, glutamine, glycine,
hydroxyproline, proline, serine, tyrosine

A

NONESSENTIAL AA

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7
Q

Found in short supply relative to need

A

“Limiting” Amino Acids

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8
Q

Have one amino group and carboxyl group

A

Neutral AA

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9
Q

Have additional NH2 group attached

A

Basic AA

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10
Q

Have additional COOH group attached

A

Acidic AA

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11
Q

Is the amino nitrogen that forms part of a ring structure

A

Imino acids

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12
Q

Give the 3 types of Neutral AA

A
  • Aliphatic AA
  • Aromatic AA
  • Sulfur-containing AA
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13
Q

Have straight or branched chains of carbon atoms & other substituents

A

Aliphatic AA

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14
Q

Amino acids that has aromatic rings attached

A

Aromatic AA

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15
Q

Amino acid that contains sulfur as a substituent

A

Sulfur-containing AA

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16
Q

Amino acid that can be catabolized or broken down to form glucose or glycogen

A

Glucogenic AA

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17
Q

Amino acid that can be catabolized to form ketone bodies

A

Ketogenic AA

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18
Q

According to Shape of Protein
- Coiled or ellipsoidal-shaped
- Insulin, albumin, globulin, etc.

A

Globular

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19
Q

According to Shape of Protein
- Helical peptide chains
- Elastin, fibrin, collagen, etc.

A

Fibrous

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20
Q

Some AMINO ACIDS can be converted to GLUCOSE via GLUCONEOGENESIS

TRUE OR FALSE

21
Q

✓ sulfur-containing amino acid formed from methionine;
✓ abundant in human milk;
✓ needed for retinal and visual function, brain development and stability of
central nervous system activity

22
Q

✓ Formed from methionine & lysine
✓ Converts acyl compounds (products of fat metabolism) to less toxic forms and removes them from the cell

23
Q

Exerts oncotic pressure for water balance

24
Q

Transports lipids

A

LIPOPROTEINS

25
Involved in immune response
GLOBULINS
26
Necessary for blood clotting
Fibrinogen
27
For muscle contraction
ACTIN AND MYOSIN
28
from dietary protein (EXOGENOUS OR ENDOGENOUS)
EXOGENOUS
29
from tissue breakdown ( EXOGENOUS OR ENDOGENOUS)
ENDOGENOUS
30
Involves the breakdown of AA into their component parts e.g. formation of glucose or KB whenever necessary
Catabolism
31
Recommended intake OF PROTEIN
10-15% OF TER
32
Give the 3 classification of AMINO ACID
ACCORDING TO ESSENTIALITY ACCORDING TO CHEMICAL PROPERTY ACCORDING TO METABOLISM
33
Give the ACCORDING TO ESSENTIALITY of Amino Acid
- Essential AA (body cannot make) - Semi-essential AA (body is inadequate to support growth and needed by young animals) - Non-essential AA ( synthesized in the body)
34
Give the ACCORDING TO CHEMICAL PROPERTY of Amino Acid
- Neutral AA (one amino group and carboxyl group) - Basic AA (additional NH2) - Acidic AA (additional COOH) - Imino acids (amino nitrogen that forms part of a ring structure)
35
Give the 3 types of Neutral Amino Acid
- Aliphatic Amino Acid (straight or branched chains of carbon atoms) - Aromatic Amino Acid (have aromatic rings attached) - Sulfur-containing Amino Acid (Contain sulfur)
36
Give the ACCORDING TO METABOLISM of Amino Acid
- Glucogenic Amino Acid (catabolized or broken down) - Ketogenic Amino Acid (can be catabolized to form ketone bodies) - Both ketogenic and glucogenic AA (Isoleucine, phenylalanine, tyrosine, tyrptophan)
37
Give the three Classification of Proteins
- According to physicochemical properties - According to Shape - According to AA Content
38
METABOLISM - Amino acids pass through PORTAL VEIN into LIVER → maintains normal levels of amino acid nitrogen in the blood (4-6 mg/dL) TRUE OR FALSE
TRUE
39
One gram nitrogen = _____ dietary protein
6.25g
40
FOOD SOURCES of AA and Proteins
ANIMAL AND PLANT SOURCES
41
Protein Deficiency leads to (Kwashiorkor or Marasmus) and what age?
Kwashiorkor (1-6 years old)
42
At nitrogen equilibrium: N ____ = N_____
INTAKE OUTPUT
43
At positive N balance: N intake (>,<) N output
- N intake > N output - Growth, pregnancy, rehabilitation from illness
44
At negative N balance: N intake (>, <) N output
- N intake < N output - Illness, malnutrition
45
Involves the incorporation of AA in the synthesis of tissue proteins
Anabolism
46
Give the three physicochemical properties of proteins
- Simple (Degraded to AA upon hydrolysis) - Compound/ conjugated (simple proteins combined with a nonprotein) - Derived (substances resulting from decomposition of simple & conjugated proteins)
47
Give the two shape of proteins
- Globular (Coiled or ellipsoidal-shaped) - Fibrous (helical peptide chains)
48
Give the three According to AA Content of proteins
- Complete (contains all the EAA) - Partially Complete (contains all the EAA but in limited amounts to support growth) - Incomplete (lacks one or more EAA)