08 Proteins & Amino Acids Flashcards

1
Q

What elements are amino acids made up of?

A

Carbon
Hydrogen
Oxygen
Nitrogen

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2
Q

What 3 sections to amino acids contain and how many known amino acids are there in nature?

A

Amine group at one end - NH2
Carboxylic group at other end - COOH
Unique side group which is different in each amino acid - denoted by R.
Approx 1,000 in nature.

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3
Q

How many amino acids are used in the synthesis of protein and how many of those are essential.
What are non-essential and conditionally essential AA’s?

A

20 build protein.
9 ar essential as the body cannot make them and needs to be obtained from diet.
Non-essential can be made by the body, conditionally essential need certain conditions and elements like vits, mins etc.

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4
Q

What are the 9 essential AA’s?

A
Histidine
Isoleucine
Leucine
Lysine
Methionine
Phenylalanine
Threonine
Tryptophan
Valine
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5
Q

What are some conditionally AA’s?

A
Arginine
Carntine
Cysteine
Glutamine
Glycine
Ornithine
Proline
Serine
Taurine
Tyrosine
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6
Q

What can denature a protein?

A

Heat, acids/alkalis, high speed mechanical mixing that disturb their structure and unravels the structure.

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7
Q

What are the 8 functions of proteins?

A

As Building materials - muscle, skin, blood, bone
As Enzymes - break/build/transform substances
As Hormones - made from cholesterol, AA’s & polypeptides
As Immunoproteins - Immunoglobulins & antibodies.
As Transport proteins
As acid base regulators
As fluid balance regulators
As conjugated proteins - joined to non-protein components.

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8
Q

Name some examples of proteins/AA’s that are made into hormones.

A

Tyrosine + Iodine = Thyroid Hormones
Tyrosine used to make dopamine, adrenaline
Tryptophan used to make melatonin

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9
Q

Name some immunoglobulins and where are they found and how are they used?

A

IgG, IgM, IgA, IgE, IgD.
Found in blood and bodily fluids.
Used to identify foreign objects.

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10
Q

Name some transport proteins and what do they carry?

A

Albumin - Ca, Zn, B6
Haemproteins - O2
Transferrin - Fe
Transthyretin+Retinol - Vit A

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11
Q

How do proteins work as acid base regulators?

A

Proteins have neg charge on surface which attract Hydrogen (+) atoms.
By accepting and release H atoms, they can maintain acid/base balance in body fluids.

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12
Q

How are proteins fluid regulators?

A

If proteins leak from capillary walls fast than they can be re-absorbed this causes swelling, oedema.

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13
Q

Give an example of a conjugated protein?

A

Glycoproteins - bound to carbs like glucose, galactose, fructose etc

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14
Q

What’s the difference between exogenous and endogenous proteins and what do they both need in addition for synthesis?

A

Exogenous - from outside dietary sources (foods)
Endogenous - from internal sources - breaking down of of body cells into amino acids for re-use.
Need nitrogen for synthesis.

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15
Q

What is transamination (and what B vitamin is needed in this) and deamination (and what substance results which is then converted into what)?

A

Transamination - Transferring/making of a non-essential amino acid into another. B6 needed.
Deamination - stripping down of proteins and nitrogen for re-use. Results in ammonia, then converted in urea by the kidneys and passed out through urine.

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16
Q

Explain how average protein requirements are calculated from nitrogen balance, and from this, what is the estimated average intake calculated to be?

A

Nitrogen needs to be balanced in the body. Measuring the amount of protein intake with nitrogen in the urine, faeces and sweat, gives an indication of the body’s balance of nitrogen.
Calculated at average of 0.83g per Kg of body weight and 1g for vegans.

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17
Q

What two things influence protein quality?

A

Amino acid content - making proteins requires all the amino acids necessary to build it.
Source of the protein.

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18
Q

What is recommended for vegetarians and vegans with regard to protein?

A

Few veg/vegan sources do not contain complete range or protein, so it’s recommended to combine two sources of protein at the same meal to complete the set of required - i.e.. rice and legumes.

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19
Q

What are some of the effects on health of excess protein (5)?

A

Heart disease - protein from animal sources usually contain high saturated fat and raises cholesterol.
Cancer - animal protein has been shown to have an effect on certain cancers.
Osteoporosis - calcium excretion is high when protein intake is high.
Weight gain - animal protein foods are often high in fat and thus higher calories, although protein is satiating, so can be useful in short term high protein diets.
Kidney disease - high protein increases kidney work (deamination-ammonia-urea)

20
Q

What are some of the effects on health of inadequate protein and what groups of people can suffer depletion?

A

Growth retardation in children.
Low energy.

Teens - junk food
Elderly - malabsorption, lack of appetite
Anorexia nervosa
Homeless

21
Q

What is the most abundant amino acid in the body, is it essential, cond-ess or non-ess, and what are it’s roles?
What neurotransmitter in the brain is it involved in?

A

Glutamine. Conditionally essential.
Fuels enterocytes, lymphocytes & microphages.
Combines with alanine to transport N in the blood.
Regulates acid/base balance.
Precursor of nucleic acids, amino sugars and glutamate.
Glutamine-glutamate-GABA.

22
Q

High levels of what, depletes glutamine stores and the generation of what immune cells are reliant on glutamine.

A

High levels of cortisol depletes glutamine stores.

Ability of lymphocytes to proliferate and generate killer cells is reliant on glutamine.

23
Q

What vegetable is high in glutamine and it’s juice is useful in what clinical application?

A

Cabbage and its juice has been shown useful in treating peptic ulcers.

24
Q

How can glutamine assist those the HIV?

A

HIV meds and damage intestine walls and lead to mal-absorption. Glutamine can correct this and improve intestinal permeability and absorption using approx 8g per day.

25
Q

How is glutamate relevant in brain health?

A

Neurotransmitter.
Precursor for GABA synthesis.
Substrate for glutathione synthesis.

26
Q

What is glutathione made from and what is it?

Why is glutamic acid not used in supplementation?

A

Tripeptide made from glutamate, cysteine and glycine.
Most abundant antioxidant in the body.

Glutamic acid can have neurotoxic effects - hence the controversial use of MSG containing it.

27
Q

What are the three main amino acids essential for the Urea Cycle, what is produced from what?
What can urea cycle impairment lead to?

A

Arginine, Ornithine, Citrulline.
Urea is produced from ammonia.
Impairment can lead to Hyperammonaemia.

28
Q

What is Arginine the precursor to and what is that involved in?
What are 3 possible clinical applications to Arginine supplementation?

A

Precursor to Nitric Oxide which is involved in endothelial relaxation, neurotransmission and thyroid activity regulator.

Help with heart disease as causes greater vasodilation
Improves sperm count/motility and helps erectile dysfunction due to vasodilation.
May accelerate wound healing.

29
Q

What are BCAA’s?

What are some of their uses and what is deficiency associated with?

A

Branched Chain Amino Acids - Valine, Leucine, Isoleucine.
Inhibits muscle breakdown during exercise and bed rest.
Deficiency associated with loss of appetite (anorexia).

30
Q

What are the two sulphur AA’s, and which can be synthesised from which?
What are they each needed for?

A

Methionine and Cysteine.
Cysteine can be synthesised from methionine.

Methionine is required for acetylcholine, adreneline.
Cysteine is required for glutathione, co-enzyme A.

31
Q

How has methionine been implicated in various diseases and what has been shown to help?

A

Implicated in hyperhomocysteinaemia and various cancers. Restriction of methionine has shown to lower homocysteine levels and also inhibit tumour growth and improve cancer treatment outcomes.

32
Q

What 4 things is methionine toxicity linked to?

A

Atherosclerosis.
Hyperhomhocysteinaemia.
Cancer.
Liver disease/cirrhosis.

33
Q

How is most sulphur in foods found, what cysteine the source of and what does sulphation do in the phase II liver detox cycle?

A

Most sulphur in food is found in the form of protein-bound cysteine.
Cysteine is the source of sulphate.
Sulphation makes hydrophobic compounds in the body more water soluble, ready for the excretion by urine.

34
Q

What important compound is a derivative of cysteine and what does this work as and help prevent?

A

N-acetyle Cysteine (NAC).

Works as an anti inflammatory and helps prevent toxic metal and chemical buildup from medications.

35
Q

How does NAC assist in HIV?

A

Can increase levels of glutathione, which reduces oxidative stress and improves the activity of CD4 T-Lymphocytes.

36
Q

What AA’s is Carnitine a derivative of and what is it’s main functions?

A

Derived from methionine and lysine and aids in cellular energy production by transporting fatty acids into mitochondria for oxidation.
Reduces surface fats like cellulite.

37
Q

What is creatine, where is 95% of it found and what is it a source of and who does it benefit?

A

A small peptide made of arginine, glycine and methionine.
Mostly found in muscle.
Source of fast energy for muscles via creatine phosphate.
Benefits athletic, muscle building performance and Parkinson’s disease sufferers.

38
Q

What is glycine’s role in the human body?

A

Synthesis of haem pigment in RBC, DNA, RNA, collagen, enzymes and transport proteins.
Detoxification.
Neurotransmitter.

39
Q

What is taurine’s role in the human body?

A
Antioxidant.
Fat metabolism.
Development of cerebellum and retina.
Bile acid.
Essential for babies.
40
Q

What is threonine’s role in the human body?

A

Found in green tea.
Calming, stress relieving.
Improves learning performance and concentration.
Lowers blood pressure.

41
Q

What is tyrosine’s role in the human body?

A

Precursor of thyroid hormones, dopamine, adrenaline.
Increases alertness.
Good for adrenal/mental exhaustion, depression, anxiety.

42
Q

What is tryptophan’s role in the human body?

A

Essential AA.
Production of B3 and serotonin.
Combats depression and insomnia.
Mood stabilising.

43
Q

What is phenylalanine’s role in the human body?

A

Essential AA.
Cross BBB.
Converts to tyrosine.

44
Q

What is lysine’s role in the human body?

A
Essential AA.
Helps build muscle.
Assists iron and zinc absorption.
Moderates triglyceride levels.
Fights herpes infection
45
Q

What are some general guidelines about AA supplementation?

A

AA compete with each other.
Long term supplementation of specific AA can lead to imbalances.
Long term AA therapy of specific AA should be done with a complete free-form AA formula.

46
Q

What are free-form amino acids?

A

Non-peptide linked AA which makes them more efficiently absorbed.

47
Q

What could be the reason for impaired AA utilisation?

A

Dietary lack of other nutrients that aid absorption, like B6, B12 and Zn etc.