Proteins Flashcards

(32 cards)

1
Q

What are the 11 functions of proteins?
(PPSTEACHERS)

A

Pigment
Poisons
Storage
Transport
Enzymes
Anti-bodies
Contractile
Hormones
Energy
Receptors
Structural

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2
Q

Where is collagen found?

A

It’s a protein found in connective tissues that provides strength. (Bone, cartilage, tendons, skin.)

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3
Q

Where is elastin found?

A

Found in connective tissue, allows the tissue to stretch. (Ligaments, lungs, artery walls.)

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4
Q

Where is keratin found?

A

Found in skin, fingernails, hair and feathers.

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5
Q

What’s the structure of an amino acid?

A

A central carbon with an amino group, a carboxyl group, and an R-group.

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6
Q

Is the variable group different for each amino acid and do they have unique chemical properties?

A

Yes!

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7
Q

What are amino acids in regards to pH?

A

Both sides of an amino acid are ionized, meaning they can act either as an acid or a base.

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8
Q

What’s a dipolar ion? Is an amino acid one?

A

A dipolar ion is a molecule that have charged groups of opposite polarity. Yes, an amino acid is one.

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9
Q

Are dipolar ions soluble?

A

Yes, they’re highly soluble in H2O.

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10
Q

Can an amino acid be just hydrophobic or hydrophilic?

A

Yes, based on their R groups.

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11
Q

What are the R group commonalities of uncharged polar amino acids?

A

They’re hydrophilic and make hydrogen bonds with H2O. Faces outwards towards H2O.

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12
Q

What are the R group commonalities of charged acidic amino acids?

A

The H’s on the carboxyl have already been donated to the solution. They’re hydrophilic.

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13
Q

What are the R group commonalities of charged basic amino acids?

A

The H’s on the amino groups have already been taken from the solution. They’re hydrophilic with a change always on N.

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14
Q

What are the R group commonalities of non polar amino acids?

A

They’re hydrophobic, making the R groups point inwards away from the water.

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15
Q

What are the R group commonalities of sulfur containing amino acids?

A

They form disulfide bridges which are covalent cross links between sulfhydryls. These stabilize the 3D structure.

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16
Q

What’s a peptide bond?

A

A covalent bond between an amine of one amino acid and a carboxyl of another. Always N to C.

17
Q

Function depends on what?

18
Q

What’s the primary structure?

A

The order of the specific amino acids as determined by genes.

19
Q

What’s the primary structure held together by?

A

Peptide bonds.

20
Q

What’s the secondary structure?

A

It’s local folding, which is interactions between adjacent amino acids.

21
Q

How is the secondary structure stabilized?

22
Q

What’s the tertiary structure?

A

Interactions between distant amino acids and environment. After the secondary structures, the rest of the chain will twist, turn and fold to satisfy the amino acid R-group.

23
Q

What’s the quaternary structure?

A

It’s more than one polypeptide chain bonded together, meaning the protein is now functional.

24
Q

What’s the arrangement of globular proteins vs structural proteins?

A

Globular : Rounded, spherical
Structural : Linear, arranged in strands or sheets.

25
What are the 6 types of bonds in the tertiary and quaternary structure?
1. Hydrogen bonds (O-H) 2. Stacking interactions (Between rings) 3. Isopeptide bonds (Between R-groups) 4. Disulfide bridges (Between 2 cystines) 5. Hydrophobic interactions (Away from H2O) 6. Ionic bonds (+ & -)
26
What is protein denaturation?
The unfolding of a protein
27
What causes protein denaturation?
The disruption of H-bonds, ionic bonds and disulfide bridges through temperature, pH and salt content.
28
What’s protein denaturation alter?
The 2* and 3* structure, which destroys and functionality.
29
Can some proteins return to their functional shape are denaturation?
Yes, but some also cannot.
30
What’s coagulation?
When protein undergoes the same conditions that cause denaturation, but they’re so harsh/long that the protein is permanently damaged and can’t ever resume function.
31
How many different amino acids do we need to consume, and how many of these can we manufacture?
20, and we can manufacture 11 from other sources.
32
What are the essential amino acids that we cannot manufacture elsewhere?
Histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan and valine.