Proteins Flashcards

(26 cards)

1
Q

What are the 4 levels of a protein structure?

A

Primary
Secondary
Tertiary
Quaternary

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2
Q

What do all the 4 levels do?

A

Interact, as well as attract or repell

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3
Q

What is the primary structure of proteins?

A

The polypeptide.

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4
Q

What is the polypeptide?

A

Amino acid sequence. Peptide bonds

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5
Q

Why are there infinite possibilities of polypeptides?

A
20 different amino acids 
Could be at any length
Amino acids can be in any order
They all have different properties
Some are polar, non polar
Some are (+) or (-) charged
Contain sulfur
Properties of amino acids determine polypeptide folds up into a protein
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6
Q

What is the secondary structure of proteins?

A

Repeated units

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7
Q

What are the repeated units? What are they held together by?

A

Alpha helixes and beta pleated sheets. H-bonds

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8
Q

What is the tertiary structure of proteins?

A

3D folded structure

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9
Q

What does the 3D folded structure have and do?

A

A hydrophobic core and folds a single protein into a 3D structure

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10
Q

What does the 3D structure give proteins?

A

Their functional properties, such as active sites on enzymes.

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11
Q

What are the R-group interactions?

A
  • Hydrophilic polar amino acids orient to the outside
  • hydrophobic non polar amino acids are protected in the core
  • oppositely-charged ions attract
  • disulfide bridges formed between sulfur-containing amino acids
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12
Q

How does the 3D create its structure?

A

With 2 or more alpha helixes, 2 or more beta pleated sheets, or one of each

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13
Q

What is the quaternary structure of proteins?

A

Multiple subunits

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14
Q

Name 3 examples of quaternary structures

A

Haemoglobin
DNA polymerase
Ion channels in the plasma membrane

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15
Q

What are fibrous proteins?

A

Insoluble on water structure
They support and strengthen
Help support the cell
The water can’t dissolve the amino acids
It’s a long and narrow structure exposing hydrophobic and hydrophilic properties

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16
Q

Name 3 examples of fibrous proteins

A
Keratin 
-hair/nails
Elastin
-skin
Collagen
-tissue strengthening
17
Q

What are globular proteins?

A
Soluble in water 
Functional 
Works as enzymes and antibodies
They can float around the cell
Amino acids stick together
They will move around the water freely
18
Q

Name 5 examples of globular proteins

A
Amylase
-digest starch
Insulin
-blood sugar regulation 
Haemoglobin 
-carries oxygen and red blood cells 
Immunoglobulins 
-immune system/defense
Na+ / K+ pump
-membrane transport
19
Q

What are some uses of proteins?

A
Hormones
-insulin
Immunoglobulin 
-antibodies
Enzymes
-catalase 
Gas transport
-haemoglobin
20
Q

What are the polar and non polar amino acids used in what kinds of channels?

A

Membrane channels

21
Q

What die the polar sections allow?

A

It allows ions to pass through. Charged or polar molecules cannot normally pass through the hydrophobic

22
Q

Where does the polar amino acids position themselves?

A

On the outside and line the protein channels for facilitate diffusion

23
Q

Where do the non polar amino acids position themselves?

A

The position themselves with the hydrophobic tails

24
Q

What does non gated mean? What does gated mean?

A

Non gated- tunnel

Gated- will cause a shape change to let things through

25
What do the non polar amino acids help do?
Bond proteins to the plasma membrane
26
What do the polar amino acids help do?
Help bind the substrates for reaction