Proteins Flashcards

1
Q

What are proteins?

A

-Principal organic chemical constituents of body organs and soft tissues
-polymers of amino acids

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2
Q

What are the functions of proteins?

A

-Membrane structure and transport
-Enzymes
-Regulation of hormones and other signaling factors
-Antibodies
-Structure

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3
Q

What are the classification of proteins?

A

Globular and Fibrous

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4
Q

What is fibrous?

A

-structure
-connective tissue

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5
Q

How do transcription and translation play a role in proteins?

A

-gene to protein
-need enough amino acids to make proteins
-DNA (transcription) -> RNA (Translation) -> Protein

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6
Q

What is the hierarchy of structural classification of proteins?

A

-Primary
-Secondary
-Tertiary
-Quaternary

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7
Q

What is the structure of a primary protein?

A

An amino acid sequence.

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8
Q

What is the structure of a secondary protein?

A

Folding of peptide regions into structures.

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9
Q

What is the structure of a tertiary protein?

A

Folding of structures into 3D shapes

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10
Q

What is the structure of a quaternary protein?

A

Multiple proteins interacting as a structure.

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11
Q

What is protein turnover?

A

-The process or rate of protein degradation
-Its significance: uses energy
-metabolic tissue higher turnover

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12
Q

What is the process of protein turnover?

A

protein ->protein degradation ->Amino Acid ->Protein Synthesis ->

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13
Q

What is Accretion?

A

Accumulating body protein

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14
Q

What is Depletion?

A

Losing body protein

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15
Q

How is accretion achieved?

A

Net gain pos

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16
Q

What is the structure of an amino acid?

A

-Amine group (NH2)
-Acid group (CHO2)
-Carbon base (CH)
-R group (side chain) makes each one special

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17
Q

What type of bond does forms protein?

A

peptide bonds

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18
Q

What happens is water is added to a peptide bond?

A

It will reverse the process back to 2 amino acids

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19
Q

What is the elemental composition of protein?

A

-Most of the mass is from carbon
-Nitrogen contributes an important protein

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20
Q

What is typically measured to determine the protein content of feeds?

A

Nitrogen because it is not in carbohydrates and identifies mostly with proteins.

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21
Q

What is the most typical description of protein composition of a feed?

A

Crude Protein

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22
Q

What is the average percent of Nitrogen in protein?

A

16% Nitrogen
-doesn’t apply to all proteins
-depends on the amino acid composition

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23
Q

How can percent N in feeds be measured?

A

Chemically

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24
Q

How do you calculate crude protein?

A

6.25 x %N = crude protein

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25
Q

Can you have a feed with over 100% crude protein context?

A

Yes, because working only with Nitrogen
-Urea 281% crude protein

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26
Q

Do animals have amino acid and protein requirements?

A

-Animals have amino acid requirements!
-No protein requirements
-some requirements are well defined and others less so

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27
Q

How many main amino acids are there?

A

20

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28
Q

Wha s an essential amino acid?

A

-something not made in the body
-need it through diet

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29
Q

Difference between plants and animals when it comes to synthesis of amino acids.

A

Plants and microorganisms can synthesize all amino acids, but animals cannot and must have dietary source of amino acids

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30
Q

For animals, how many amino acids must be obtained through the diet?

A

8 must be obtained through the diet out of the 20-25 amino acids in animal tissue.
-All species!

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31
Q

How many essential amino acids are needed for growing pigs?

A

10

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32
Q

What amino acid do chickens not synthesize?

A

Glycine, because of this it is considered essential

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33
Q

What are the 10 essentia amino acids?

A
  1. Phenylalanine
  2. Valine
  3. Threonine
  4. Tryptophan
  5. Isoleucine
  6. Methionine
  7. Histidine
  8. Arginine
  9. Leucine
  10. Lysine
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34
Q

Do ruminants absorb protein in the rumen?

A

No, different from carbohydrate absorption, rumen bacteria does get first pass on dietary protein, but protein exits the rumen for digestion by the same mechanisms as non-ruminants.

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35
Q

Process of dietary protein in non-ruminants

A

dietary protein -> acid stomach -> small intestine

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36
Q

Process of dietary protein in ruminants

A

dietary protein -> rumen -> acid stomach -> small intestine

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37
Q

Are ruminants and non-ruminants the same once at a certain point?

A

Yes, once at the acid stomach the process is the same for non-ruminants and ruminants

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38
Q

Does rumen bacteria modify dietary protein?

A

Yes, it affects the protein structures and uses the protein, but proteins still exit the rumen (some as feed and some as bacteria protein)

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39
Q

Where is the initiation of the acid stomach in non-ruminants, ruminants, and birds?

A

-Non-ruminants: Stomach
-Ruminants: abomasum (bottom right side)
-Birds: proventriculus

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40
Q

What does the acidic stomach provide?

A

-acid (HCl)
-proteolytic enzyme: non-specific and chew up anything
-pepsin reduce large polypeptides to smaller polypeptides

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41
Q

What do pancreatic enzymes do?

A

-continue reduction in the size of polypeptides
-Multiple enzymes secreted into the small intestine

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42
Q

What pancreatic enzymes are secreted into the small intestine?

A

-Trypsin (cut specific AA)
-Chymotrypsin (cut specific AA) and carboxypeptidases (cleaves carboxy groups)
-Elastase ( cleaves elastoses)
works in acidic pH

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43
Q

What are the end products of pepsin digestion?

A

Substrates

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44
Q

What is used in protein digestion in the small intestine?

A

Brush Border Peptidases

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45
Q

What is the process of the Brush Border Peptidase?

A
  1. Reduce tetra-peptides and larger to single amino acid and di- and tri-peptides.
  2. Cleaves single amino acids from ends as well as interior peptide binds depending on the peptidase.
    -Examples: endopeptidase (works in the middle)
    -aminopeptidase (works on the end)
    -carboxypeptidases
    -dipeptidases
  3. Many are metalloenzymes (contains metal ion)
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46
Q

Why are peptidases from proline containing peptides difficult for pancreatic enzymes?

A

Because proline has an amine group shaped in a ring
-enzymes don’t work as effectively

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47
Q

What are the types of transporters for absorption into enterocytes?

A

-Amino acid transportERS
-Protein transportER

48
Q

How do Amino Acid TransortERS work?

A

-Many transporting chemically similar groups of amino acids
-many transporters transporting a single amino acid
-specialization
-Active transport: Gradients (Na, K, Cl) and uses energy through ATP

49
Q

How does Peptide TransportER work?

A

-PepT1
-Transport di- and tri- peptides: Two or three amino acid peptides
-Energy through H gradient
-PepT1 no specialization
-transport 2 or 3 at a time
-Efficient!

50
Q

Why are both amino acid and peptide transport used?

A

because there might already be single amino acids broken down by the stomach
-further down the GI tract the more likely to have individual amino acids

51
Q

Where does absorption of amino acids happen?

A

Small Intestine

52
Q

What is digestibility?

A

How much nutritionwe can absorb

53
Q

Why measure digestibility?

A

How much is actually being absorbed

54
Q

How can we measure digestibility?

A

-Apparent digestibility: Intake - Output = absorbed
-Influence of digestive physiology

55
Q

What nutrients are easy to measure? and which are challenging to measure?

A

-Fiber digestibility is easy to measure because we use apparent digestibility
-Amino acids are challenging to measure because in ruminates bacteria from the rumen contain nitrogen and make protein digestibility look higher than it really is.

56
Q

Do proteins that exist the small intestine be absorbed as amino acids?

A

No

57
Q

Does bacteria in the large intestine, containing protein, contribute to amino acid absorption?

A

No

58
Q

How are amino acids measured?

A

Measuring amino acids at the ileum indicates what was absorbed
-true ileum amino acid digestibility reflects disappearance (absorption) of dietary amino acids and accounts or endogenous contributions
-Uses a port/canula

59
Q

What happens to amino acids after absorption?

A

Amino acids are released into blood from enterocytes

60
Q

What vein drains blood from the intestines? and where does it go?

A

-Portal vein
-blood supply leaving the gut goes to the liver through the portal vein
-blood flows to the liver before returning to the venous circulation

61
Q

What happens when blood goes through the liver?

A

-The liver can use and process nutrients from the blood including amino acids and glucose
-The blood than goes onto venous circulation and peripheral tissue

62
Q

How many pounds are in a short ton?

A

2,000 Ibs in a shirt ton

63
Q

How many kg ina metric ton?

A

1,000 kg in a metric ton

64
Q

How many pounds in a kg

A

2.2 Ibs in a kg

65
Q

Overall process of protein metabolism

A
  1. Protein translation: using amino acids for protein synthesis
  2. Non-essential amino acids: synthesize it
    -Essential amino acids: stuck/can’t do anything
  3. Deamination: remove NH2 and produce NH3 (ammonia)
  4. Detoxify: Urea synthesis
66
Q

Wat are the potential fates of circulating amino acids after cell uptake?

A

-Substrate for neurotransmitter synthesis
-Protein synthesis by peripheral tissue
-Amine donor for non-essential amino acids synthesis
-Deamination to provide carbon skeleton donor for gluconeogenesis
-Energy production: Oxidation

67
Q

What do amino acids used in translation produce?

A

Proteins with amino acids linked by peptide bonds

68
Q

Translation from the mRNA transcript

A

-tRNA binds to matching codon
-the polypeptide is linked to the new amino acid
-mRNA is shifted forward, exposing a new codon
(3 nucleotide codon)

69
Q

What are the steps in protein translation require energy?

A

-Amino acid activation
-Initiation of peptide chain formation
-Peptide chain elongation
-Termination of polypeptide synthesis

70
Q

What is the relative ratio of ATP mols per protein mols?

A

-5 mol ATP per 1 mol protein
-A mol of protein can be thought of as 100-120g of protein

71
Q

How many mol ATP per mol protein does amino acid transport require?

A

Amino acid transport into cells requires approximately 0.5 mol ATP per 1 mol protein is required.

72
Q

Ratio of mol protein to mol glucose?

A

1 mol protein to 1 mol glucose

73
Q

Synthesis of Non-essential amino acid (NEAA)

A

-making new amino acids from other amino acids and carbon skeleton
-Essential amino acids can provide the amino group needed for the NEAA synthesis
-can also provide carbon skeleton for synthesis of many NEAA

74
Q

Can all cells and tissues create the amino acids they need?

A

No, not all cells and tissues can complete conversions
-Some cells or tissues lack a key enzyme for certain amino aids: in combination, tissues have the capacity to synthesize NEAA (EAA donates for NEAA)

75
Q

What is turnover?

A

Tissue somewhere amino acid and put into circulation for other to use

76
Q

What is transamination reaction?

A

-moving an amino group to make a keto acid
-uses aminotransferase
-Shifting the amino acids we have to make ones we need

77
Q

What is Deamination?

A

-removing of an amino group
-produces NH3 (ammonia) and a ketoacid
uses the enzyme L amino acid deaminase (L-AAD)

78
Q

What are ketoacids? and what happens to them after and deamination?

A

-caron skeleton
-can be further metabolized in many pathways to produce other products
-products and pathways depend on individual amino group

79
Q

What should I know about the Kerbs Cycle?

A

The carbon in an amino acid can be used in many pathways.

80
Q

What does the Urea cycle do?

A

Dispose of ammonia

81
Q

How is ammonia produced?

A

-Oxidation of amino acids produces NH3
-Ammonia is essential to life for many reactions, but an excess is toxic!

82
Q

How is ammonia removed?

A

-urea synthesis by the liver: urea is water soluble and non-toxic, and can be excreted in urine
-Liver removes ammonia from the blood as well as intracellular ammonia produced in the hepatocytes of the liver

83
Q

Outline of feeding requirements

A
  1. Influence on protein requirements
  2. Nutrient Requirements
    -For growth, composition of gain influences requirements
    ~composition = fat vs lean
    -Production also influences requirements
  3. Protein or amino acid requirements
  4. Feed amino acids supplies
84
Q

What is the percent of water in lean tissue?

A

75%

84
Q

What is the percent water in adipose tissue?

A

20%

85
Q

Does the gain of body tissue have different requirments?

A

Yes, depends on composition

86
Q

Does lean tissue gain bring in water? how much energy is needed?

A

-Lean tissue gain brings water with it
-Less energy needed per unit of lean gain because no energy needed for water gain

87
Q

Does adipose tissue gain bring in water? how much energy is needed?

A

has less water
-needs more energy per unit of gain

88
Q

What is needed to make lean tissue?

A

Protein

89
Q

What type of tissue do younger animals accrete more of?

A

Gain more lean tissue (muscle) as a proportion of their body weight

90
Q

In older animals what is a greater proportion of their body weight gain?

A

Fat

91
Q

What is empty body weight?

A

Body weight with NO organs

92
Q

On a graph what happens to the body protein line when body weight increases?

A

The body protein line plateaus with increasing body weight

93
Q

Is water proportional to protein on a graph?

A

Yes

94
Q

Does fat plateau on a graph when body weight increases?

A

Fat does not plateau

95
Q

What is missing in a body composition graph?

A

Missing bone Weight

96
Q

What do older animals gain more easily?

A

Fat

97
Q

How much protein or fat is gain in younger and older animals in 1 kg of gain?

A

-In older animals 1 kg of gain is mostly fat
-In younger animals 1 kg of gain is mostly protein

98
Q

What is ADG?

A

Average daily gain

99
Q

What is the trend in ADG?

A

-As weight increases percent amount of protein decreases
-As weight increases percent amount of fat increases

100
Q

Do protein requirements change in milk production?

A

As lactation progresses and milk production changes, the protein requirements needed to support milk product changes.

101
Q

What is the required amino acid concentration for eggs?

A

-Required amino acid concentration in diet at 80 g/day intake
-At 90% egg production (90 eggs per 100 hens daily)

102
Q

Ruminant amino acid requirements

A

-Rumen gets first pass on feeds
-microbes modify and alter amino acid profiles ad they make their proteins

103
Q

How is important is the amino acid profile of feed in ruminants?

A

Amino acid profile of feed is not very important because bacteria modifies the protein and makes it the high quality amino acid that is needed.

104
Q

Do feedstuff proteins have variable amino acid profiles?

A

Yes, feedstuff have variable amino acid profiles across feed not just protein concentration variation.

105
Q

What is the protein quality determined by?

A

Amino acid profile of the feed and the digestibility of the protein.

106
Q

Do plant proteins used in feed tend do have a EAA deficiency? if so how is this solved?

A

Yes, Plant proteins tend to have some EAA deficiencies that can be over some using mixtures or with inclusion of animal source protein or amino acid supplements.

107
Q

Should the protein in feedstuff match the need of the animal?

A

Yes, they better a protein matches the need of an animal the higher quality of feed it is.

108
Q

How should you find out soybean amino acid composition?

A

Refer to analysis of a feed or a table value from a reference

109
Q

What do microbes in the rumen include?

A

-bacteria
-protozoa
-some fungi

110
Q

How do rumen microbes use feed protein?

A

Use feed protein amino acids to synthesize their own microbial protein including interconversion of amino acids

111
Q

How does microbial protein compare to requirements?

A

Take low quality protein and convert them to higher quality/needed amino acids

112
Q

What is amino acid concentration?

A

A percentage of total amino acids in rumen bacteria found floating in rumen fluid and bacteria found attached to feed particles in the rumen.

113
Q

What is considered a good quality for dairy cattle and why?

A

-Mixed microbial protein
-because of high apparent digestibility and EAA composition similar to that of lean body tissue and milk

114
Q

What does rumen protein synthesis provide?

A

At least half of the amino acids for the synthesis of milk and meat in ruminants