Protein Study Flashcards

1
Q

what are proteins?

A

essential components of animal tissue

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2
Q

chemically, amino acids consists of?

A

alpha carbons
amino groups
carboxyl group
side chains

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3
Q

how many AA are there

A

300

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4
Q

how many AA used for protein synthesis

A

20

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5
Q

2 isomeric forms AA can exists

A

D and L isomers

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6
Q

key points of L-isomer

A

only one used in proteins
used nationally
D made into L to make protein

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7
Q

proteins are macromolecules of?

A

amino acid chain

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8
Q

Amino acids classified based on

A

Structure
Essentiality
Polarity
Electrical Charge

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9
Q

what is important about each characteristics

A
structure = distinct side chain
Essentiality = dietary requirements 
Polartiy = non-polar v polar
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10
Q

Structure and Essentiality similarities

A

side chain determines if AA are synthesized by mammalian cells

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11
Q

Polarity

A

when AA interact with water at physical pH

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12
Q

electrical charge

A

charge of amino acid in aqueous solution at physical pH

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13
Q

what synthesizes amino acids

A

microbes

diet (plants)

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14
Q

what doesn’t synthesizes amino acids

A

animals

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15
Q

amino acids essential and non-polar

A
valine
methionine
leucine
tryptophan
isoleucine
phenylalanine
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16
Q

amino acids nonessential and nonpolar

A

glycine
alanine
proline

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17
Q

amino acids essential and polar

A

arginine
histidine
lysine
theronine

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18
Q

amino acids nonessential and polar

A
tyrosine
cysteine
serine
aspartate
asparagine
glutamate
glutamine
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19
Q

amino acids that are branched

A

valine
leucine
isoleucine

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20
Q

sulfur containing amino acids

A

methionine

cysteine

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21
Q

amino acids considered aromatic

A

trytophan

phenylalanine

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22
Q

which amino acids transport nitrogen

A

aspartate

glutamate

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23
Q

what amino acid in pigs and chicken with corn

A

Lysine

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24
Q

amino acids not branched

A

Theronine

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25
Q

what is wrong with Proline?

A

digestive issues due to Nitrogen side chain

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26
Q

what are essential amino acids?

A

required in diet and mammalian cells can’t synthesize proper amounts

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27
Q

what are limiting amino acids?

A

EAA that are limited in diet

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28
Q

what are non-essential amino acids?

A

not required in diet due to mammalian cells making sufficient amounts

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29
Q

why is arginine considered semi-essential?

A

can be synthesized in body NOT in proper amounts

30
Q

limiting amino acids in ruminants

A

Methionine

31
Q

limiting amino acids in pigs

A

Lysine

32
Q

what are protein chains made of?

A

amino acids

33
Q

amino acids linked by?

A

peptide bonds

34
Q

what are dipeptides?

A

2 amino acids linked

35
Q

what are polypeptides?

A

greater than 10 amino acids linked

36
Q

what are protein synthesis based on

A

genetic code

37
Q

what’s transcription?

A

DNA code copied to mRNA

38
Q

what’s translation?

A

mRNA used to assemble an amino avid chain

39
Q

what biological properties of protein does genetic code determine

A

AA protein contain
AA sequence
length of AA chain
spatial relationship of AA within protein

40
Q

what protein is made with high levels of cystine

A

keratin

ex. hair

41
Q

4 levels of structural organization in proteins

A

Primary
Secondary
Tertiary
Quartenary

42
Q

what does the primary structure consists of

A

sequence of amino acids linked by peptide bonds

43
Q

what does secondary structure consists of

A

coiling of folding polypeptide chains to alpha-helix/beta-pleated sheets from H bonds

44
Q

what does the tertiary structure consists of

A

3-D folding of chain by H bonds and electrostatic attractions

45
Q

what does the quartenary structure consists of

A

protein macromolecules formed by polypeptide chains by H bonds and electrostatic attraction

46
Q

how are proteins classified

A

based on composition, solubility, nutritive value, shape, size and function

47
Q

microbes provide how much protein for ruminants

A

50 - 80%

48
Q

what is the ultimate goal of protein digestion?

A
  • pieces of food converted to smaller digestible portions

- hydrolysis of peptide bonds to produce free AA

49
Q

what does digestive enzymes do?

A

break peptide bonds

50
Q

name of digestive enzymes secreted as inactive pro-enzymes

A

zymogens

51
Q

what is exopeptidases?

A

cleave amino acids at terminal end of protein molecules

52
Q

what is endopeptidases?

A

hydrolyse peptide bonds within primary protein structure

53
Q

Characteristics of HCl in protein digestion

A
  • released from parietal cells
  • pH = 1.6 - 3.2
  • Denatures 4, 3 and 2 structures
54
Q

Characteristics of Pepsiogen in protein digestion

A
  • released from chief cells

- works with HCl to become pepsin

55
Q

Characteristics of Pepsin in digestion

A
  • Endopeptidase

- cleaves side of amino side of aromatic AA

56
Q

active form?

inactive form?

A
active = pepsin
inactive = pepsinogen
57
Q

pH of small intestine in non-ruminant protein digestion

A

7 - 8

58
Q

pancreatic enzymes secreted in small intestine of non-ruminant

A
Trypsinogen
Chymotrypsinogen
Procarboxypeptidase
Proelastase
Collagenase
59
Q

Intestinal brush border enzymes secreted

A

Aminopeptidases

Dipeptidases

60
Q

Trypsinogen activated by and converted to

A
Activated = Enteropeptidase
Converts = Trypsin
61
Q

Chymotrypsinogen activated by and converted to

A

Activated = Trypsin

Converted –> Chymotrypsin

62
Q

Procarboxypeptidase activated by and converted to

A

Activated = Trypsin

Converted –> Carboxypeptidase

63
Q

where does aminopeptidase cleave

A

Nitrogen terminal of AA

64
Q

dipeptidases cleave what?

A

dipeptides

65
Q

what are proteins broken down to?

A
  • Tripeptides
  • Dipeptides
  • Free AA
66
Q

Characteristics of Trypsin inhibitors?

A
  • small proteins & peptides
  • inactivated by heat
  • block digestion of proteins
  • found in plants, organs and fluids
67
Q

Ruminally Degradable Proteins

A

proteins available to the rumen microbes

68
Q

Ruminally Undegradable Protein

A

protein that escapes rumen fermentation and goes to small intestine

69
Q

Non Protein Nitrogen

A

not true protein providesa source of Nitrogen

70
Q

Microbes break down dietary proteis

A
  • amino acids
  • NH3
  • VFAs
  • CO2
71
Q

Factors that affect ruminal degredation

A
  • Heat Treatment
  • Rate of Passage
  • N and S availability
  • Energy availability