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AVS 305 > Protein > Flashcards

Protein Flashcards

1
Q

What type of bonds do proteins form?

A

peptide bonds

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2
Q

What are some examples of proteins?

A

canola seed, canola meal, soybean, dry distillers grains, corn gluten meal, and urea.

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3
Q

What are amino acids?

A

building blocks for protein

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4
Q

What do amino acids consist of?

A

amino group, carboxyl group, hydrogen, and side chain

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5
Q

nonpolar=

A

hydrophobic

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6
Q

polar=

A

hydrophilic

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7
Q

What is a protein?

A

biopolymer made up of repeating units of amino acids linked to each other by a peptide bond

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8
Q

what type of bond contains 2 amino acids?

A

dipeptide

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9
Q

what type of bond contains 3 amino acids?

A

tripeptide

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10
Q

what type of bond contains 2-20 amino acids?

A

oligopeptides

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11
Q

what type of bond contains 20 or more amino acids?

A

polypeptides

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12
Q

what is an essential/indispensable amino acid?

A

an amino acid that cannot be synthesized, therefore must be supplied in the diet.

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13
Q

how many essential amino acids are there?

A

8-10 depending on the species and physiological state

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14
Q

What are 4 common essential amino acids?

A

Lysine, Methionine, Valine, Tryptophan

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15
Q

what is methionine?

A

sulfur containing acid
most limiting amino acid
**if there is enough methionine, it can synthesize cysteine.

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16
Q

Lysine+Methionine-

A

cysteine

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17
Q

What is a nonessential/dispensible amino acid?

A

amino acids that the body can synthesize.
if you do not have enough of these, it can increase your need for essential amino acids.
there are 10-12 NEAA

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18
Q

Name 4 non-essential amino acids

A

Cysteine
Alanine
Glutamine
Proline

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19
Q

What is a conditionally essential amino acid?

A

Their synthesis can be limited under certain conditions.

Ex- Glutamine, Tyrosine

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20
Q

Name 3 conditionally essential amino acids

A

tyrosine, cysteine, glutamine

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21
Q

How to read the Liebigs Barrel

A

shortest stave=1st limiting amino acid

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22
Q

What is biological value?

A

the ability of a specific dietary protein to supply amino acids in the relative amounts required for protein synthesis by body tissues.
It is influenced by essential amino acids. It is fixed

23
Q

How is protein synthesized?

A

DNA-Transcription-Translation-Phenotype

24
Q

What is transcription?

A

converts DNA to mRNA

25
Q

What is translation?

A

converts info in mRNA to a polypeptide chain.

26
Q

what is cell signaling of protein synthesis?

A

cell first receives signals
up or down regulation
-turning of protein on or off

27
Q

what is a gene?

A

a region of DNA that encodes a functional RNA or protein product

28
Q

What is a complete protein

A

contains all AA you need

29
Q

what is an incomplete protein?

A

doesn’t have all required AA for protein synthesis

30
Q

What is a high quality protein?

A

complete protein

contains adequate amount of AA

31
Q

what is a low qualtity protein?

A

lacks one or more essential amino acid

32
Q

What is nutritive value determined by?

A

digestibility

33
Q

primary structure in nutritive value

A

amino acid polypeptide chain

34
Q

What is nutritive value related to?

A

folding of protein

35
Q

What is the product of altering protein quality?

A

genetic modification and engineering
GMO’s
contains protein with more lysine and tryptophan

36
Q

Protein Structure

A 
"form follows function"
order of AA in chain
length of polypeptide chain
interactions within chain, between chains, with other components 
-folding, interfolding, coiling
37
Q

order of structures

A

primary, secondary, tertiary, quaternary

38
Q

What is the primary structure?

A

the sequence of amino acids in a single polypeptide chain

  • it is critical to protein function
  • impacts nutritive value through EAA composition and chemical and physical properties
39
Q

what is the secondary structure?

A

folding of a protein as a result of hydrogen bonds that form between carboxyl and amino groups in the peptide backbone

common patterns: alpha-helix and beta-folded sheets

40
Q

what is the tertiary structure?

A

3-dimensional folding and coiling of polypeptide chain into globular structure caused by hydrogen bonds, ionic bonds, disulfide bonds, hydrophobic interactions

41
Q

what is the quaternary structure?

A 
interactive interfolding of several polypeptide chains to form a single functional protein
function determined by: shape, components
42
Q

what does hemoglobin transport?

A

oxygen

43
Q

what are some diseases of improper folding?

A

sickle cell anemia, cystic fibrosis, cancers, alzheimers

44
Q

what is denaturation?

A

change (unfolding and unraveling) in protein tertiary and quaternary structure caused by physical agitation, heat, acid, and alcohol

45
Q

what are some biological functions of proteins?

A

structural and mechanical roles, catalysis, cell signaling and immune function, fluid balance and pH regulation, transport, source of energy

46
Q

what are examples of structural role in biological functions?

A

collagen, keratin

47
Q

what are examples of mechanical role in biological functions?

A

motor proteins (make muscles work)

48
Q

what is catalysis?

A

proteins that speed up (catalyze) chemical reactions without being used up or destroyed in the process

ex: amylase, lactase, cellulase, sucrase

49
Q

What do hormones have to do with cell signaling?

A

chemical messengers that are made in one part of the body but act on cells in other parts of the body

ex: insulin, testosterone, estrogen

50
Q

immune function

A

immunoglobulins, antibodies
y-shaped proteins that attack and inactivate bacteria and viruses that cause infection

ex of immunoglobulins: igg, iga, igm

51
Q

what is fluid balance?

A

movement of fluid between intravascular and interstitial space dependent on:
pumping action of heart, osmotic pressure, albumin

52
Q

what is an edema?

A

disruption of body fluid balance

fluid build up in the limbs

53
Q

transport proteins

A

transport substances across cell membranes, transport substances in blood
ex: hemoglobin (transports oxygen) and lipoproteins (transports lipids)

AVS 305 (9 decks)

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