Proteins Flashcards

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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
Q

What do the non polar amino acids help do?

A

Bond proteins to the plasma membrane

26
Q

What do the polar amino acids help do?

A

Help bind the substrates for reaction