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Cnm N1 Semster 2 > Proteins > Flashcards

Proteins Flashcards

1
Q

Proteins accounts for how much body weight?

A

17%

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2
Q

What do amino acids contain

A

-Carboxylic acid
-Amino group
-Unique R group which differentiates amino acids

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3
Q

What are the 9 essential amino acids think PVT TIM HiLL

A

Phenylalanine
Valine
Threonine
Tryptophan
Isoleucine
Methionine
Histidine
Leucine
Lysine

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4
Q

Name 5 protein functions

A

Structure of body tissues (collagen)

Movement (actin and myosin)

Carrier molecules (haemoglobin)

Storage molecules (ferritin for Iron)

Fluids balance in blood (albumin)

Enzymes

Hormones (insulin) and cell membranes

Immune functions (antibodies)

Clotting mechanisms (clotting factors)

Alternative energy source

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5
Q

Name the 5 glycoproteins

A

Mucins (protective lubrecating barrier)

ABO blood type antigens

Hormones (LH,FSH,TSH)

Major histocompatibility complex (cell surface receptors involves in adaptive immunity)

Proteoglycans (subclass of glycoprotein ) are bound to glycosaminoglycans found in extra cellular matrix.
Shock absorbers

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6
Q

what is protein deamination?

A

Deamination = removal of the nitrogen-containing amino group
from amino acids and occurs primarily in the liver.
*When the nitrogen group is removed from the amino acid, ammonia is formed which is very toxic. To then
convert the ammonia to a water-soluble compound, it must go through a series of transformation reactions in the liver known a the ‘urea cycle’ to ensure that it can be excreted by the kidneys.
The less toxic, water-soluble compound formed is ‘urea’,
which is filtered out by the kidneys as part of urine.

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7
Q

remaining fragments of amino acids after deamination can be used to produce what ?

A

glucose and ketones

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8
Q

what is the urea cycle?

A

Ammonia formed by deamination needs to be converted to
‘urea’ to ensure its safe removal from the body. This involves
the Urea Cycle, which takes place in hepatocytes (liver cells).

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9
Q

explain transamination

A

This is an important step
in the synthesis of some
non-essential amino acids. If a particular non-essential amino
acid is not available, the body can make it from another.
* The amino group of an amino acid is transferred onto an
enzyme. The enzyme then transfers the amino group
on to a ketoacid, thus forming the new amino acid.

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10
Q

what vitamin is transamination dependent on?

A

B6

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11
Q

how would you optimise protein digestion?

A

-Chew thoroughly and avoid drinking with meals.
- Support stomach acid levels with Zinc and B6-rich foods.
– Apple cider vinegar in a little water before meals.
– Bitter herbs and foods before meals
(These also promote the release of pancreatic juice.)
– Use betaine hydrochloride supplements

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12
Q

what happens to undigested protein

A

The microbiome contributes to protein metabolism: undigested
protein that reaches the colon is fermented, creating toxic
metabolites that increase the inflammatory response and
encourages the proliferation of opportunistic pathogens

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13
Q

what are the 4 limiting amino acids?

A

lysine, threonine, methionine, and
tryptophan

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14
Q

what % of protein in the diet is considered excess

A

20%

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15
Q

why would excess protein cause cancer?

A

Polycyclic
aromatic hydrocarbons (PAHs) and heterocyclic amines (HCAs)
produced during the high temperature cooking of meat
(e.g. frying, BBQ, high temp-roasting)are carcinogenic.

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16
Q

2 reasons why excess protein would cause skeletal diseases

A

1)due to the acidic burden of excess animal protein, it can also
draw calcium out of bones and increase the risk of osteoporosis.
2) because of the collagen structure within bone, a protein deficiency can also negatively impact bone health.

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17
Q

why would excess protein cause cardiovascular issues

A

because of the oxidation and inflammation of the endothelium

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18
Q

why would excess protein cause kidney disease

A

The extra acidity from a high animal protein
intake needs buffering by the kidneys. The kidneys
must also filter the increased urea that is generated.

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19
Q

apart from protein building what other jobs do amino acids have name 4?

A
  • Contribute to the synthesis of hormones and neurotransmitters.
  • Act as neurotransmitters themselves e.g. glycine.
  • Act as methyl donors e.g. methionine.
  • Build bile acids for digestion (glycine and taurine).
  • Act as precursors for nitric oxide production e.g. Arginine.
  • Help detoxify thousands of chemicals (i.e. phase 2 liver pathways).
  • Act as precursors for the manufacture of endogenous antioxidants.
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20
Q

what amino acid is t is the preferred fuel for rapidly dividing cells such as enterocytes, lymphocytes and macrophages

A

Glutamine

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21
Q

what does glutamine do to intestinal cells

A

helps to regulate tight junction integrity and enterocyte proliferation.
.

22
Q

why would you tell someone to drink 1 litre of cabbage juice for 10 day

A

because its high in glutamine which supports intestinal permeability

23
Q

how does glutamine affect neurotransmitters and support anxiety

A

Glutamine is converted to glutamate (excitatory),
before being converted to GABA (inhibitory). The conversion from glutamate to GABA requires vitamin B6, taurine and zinc. If this conversion is operating
well, glutamine supplementation can have an anxiety-relieving, sleep supporting effect.

24
Q

what amino acid is s a substrate for
gluconeogenesis.

A

Glutamine

25
Q

what conditionally essential amino acid formed from
methionine and serine in the liver and what vitamins are needed for this conversion

A

cysteine , B6, B9 and B12 are needed.

26
Q

what amino acid is It is a component of glutathione and is needed
in the formation of Co-enzyme A and taurine.

A

cysteine

27
Q

why is cysteine crucial for drug metabolism.

A

drugs deplete glutathione – cysteine
regenerates it.

28
Q

how does cysteine help in respiratory problems.

A

it breaks up mucus to aid easier elimination from the respiratory tract.Mainly due to the breakage of the disulphide bonds in mucoproteins.

29
Q

how does cysteine impact male fertility

A

Has been shown to increase sperm
concentration, likely due to its
antioxidant properties.
Positively impacts serum testosterone

30
Q

what is the function of methionine

A

Methionine is a major methyl donor in the body (for
methylation reactions such as the homocysteine cycle, and in
phase 2 liver detoxification).

31
Q

what is the main function of carnitine

A

Carnitine facilitates the
transport of long-chain fatty
acids across the
mitochondrial membrane so
they can be oxidised (‘burnt’)
to create ATP.
* Its also removes potentially
toxic metabolites out of the mitochondria

32
Q

what is the first molecule to
be depleted in cardiac ischaemia

A

Creatine

33
Q

where is 95% of creatine found

A

the muscles

34
Q

what is glycine made with the help of ?

A

serine and B6

35
Q

what amino acid is 1/3 of collagen made from

A

Glycine

36
Q

what can glycine be reversibly converted to to create acetylcholine

A

serine

37
Q

How does glycine suport the Liver

A

-Required to conjugate toxins in phase 2
liver detoxification.
-Glycine is a component of the tripeptide
glutathione, as well as bile acids.

38
Q

what amino acid is sythesisied from cysteine vitamin B6.

A

taurine

39
Q

Supplementation is necessary in non-breastfed infants
because their ability to synthesise ………. is undeveloped
and cow’s milk does not provide a sufficient amount.

A

taurine

40
Q

what amino acid plays an important role in the contraction of muscles

A

taurine

41
Q

explain how Theanine works

A

After ingestion, theanine crosses
the blood brain barrier and blocks
glutamate receptors, whilst
increasing GABA activity. GABA is
inhibitory / calming.
-Increases alpha-brain waves
producing a calming, moodenhancing effect without
drowsiness.
-Has been shown to increase seritonin and dopimine receptors

42
Q

what is high in Theanine

A

Green tea

43
Q

what amino acid is Approved for the treatment
of congestive heart failure in Japan.

A

taurine

44
Q

How does tyrosine support endocrine health

A
  • Tyrosine is a precursor to the
    thyroid hormones, dopamine,
    epinephrine (adrenaline),
    norepinephrine (noradrenaline).
  • It is also a precursor to melanin
    (the skin pigment).
45
Q

why would low serotonin cause carbohydrate cravings

A

Tryptophan which is used for synthesis of serotonin is assisted across the blood brain barrier by insulin so low
serotonin levels cause
carbohydrate cravings as the brain is looking for ways of getting more tryptophan to it

46
Q

why would you supplement H-TP5 instead of tryptophan for neorlogial problems

A

because then the body will only used only for serotonin and melationin production as tryptophan supplementation can be used for other things such at protein synthesis and B3 formation

47
Q

give 2 examples of how Phenylalanine can be used

A

endocrine health-Can be converted to
tyrosine→ thyroid
hormones, dopamine,

skin Pigmentation
* Melanin production (via
tyrosine pathway)

48
Q

Explain how Lysine supplementation works with the herpes simplex virus

A

Lysine is the sister amino acid to arginine (they compete for absorption). The herpes simplex virus uses arginine to replicate, so
increases in lysine can limit viral replication .supplimting with vitamin C makes it more effective

49
Q

what amino acid Lysine aids intestinal absorption
of calcium, iron and zinc.

A

Lysine

50
Q

Name one function of arginine

A

Aginine is a
precursor to Nitric
Oxide. Nitric oxide
is a vasodilator and
subsequently
lowers blood

51
Q
A

Cnm N1 Semster 2 (2 decks)

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