Proteins Flashcards

(38 cards)

1
Q

Define:

Metabolic

A

All the biochemical reactions that happen inside the cells of an organism

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2
Q

Define catabolic reactions

A

Breaking down large molecules (hydrolysis)

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3
Q

Define anabolic reaction

A

Building large molecules (condensation )

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4
Q

What’s the monomer and polymer for:

Carbohydrates

A

Monomer- monosaccharides

Polymer- polysaccharides

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5
Q

What’s the monomer and polymer for:

Proteins

A

Amino acids

Polypeptide

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6
Q

What’s the monomer and polymer for:

Nucleus acids

A

Nucleotide

Polynucleotide

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7
Q

What is hydrolysis used for

A

To remove a monomer from a polymer

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8
Q

What is condensation reaction used for

A

To add a monomer to a polymer chain + WATER IS PRODUCED

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9
Q

Condensation:

  • makes a ____________
  • a new covalent bond is __________
  • a water molecule is ___________

For example

A

Polymer

Formed

Released/made

Protein synthesis

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10
Q

Hydrolysis:

  • makes a ____________
  • a new covalent bond is __________
  • a water molecule is ___________

For example

A

Monomer

Broken

Is used

Digestion

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11
Q

H R O
\ | //
\ | //
N—

A
R = r group 
H-N-H = amine group
C= central carbon atoms 
O=C-OH= carboxylic acid group
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12
Q

What is a dipeptide reaction

A

A condensation reaction where a peptide bond is formed

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13
Q

List the 4 types of protein structure

A

Primary

Secondary

Tertiary

Quaternary

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14
Q

Define primary structures

A

The specific sequence of amino acids in a protein chain

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15
Q

What is secondary structure

A

The coiling and pleating of parts of the polypeptide chain to form an alpha helix or a beta pleated sheet - held together by hydrogen bonds

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16
Q

What is the tertiary structure

A

When the secondary alpha helix and beta pleated sheet folds further to give a complex and specific 3D shape

Has hydrophobic and hydrophilic parts

17
Q

How does the tertiary structure denature

A

Heat gives kinetic energy which causes hydrogen bonds to break and the 3D structure to unravel

18
Q

What do r groups cause

A

Folding - due to hydrogen bonds ionic bonds and disulphides bonds

19
Q

What is a quaternary structure

A

Proteins with more than one polypeptide chain

2 alpha 2 beta

20
Q

In a quaternary structure what does each chain have

A

A haem prosthetic group which contains an Fe2+ ion

21
Q

Name 3 examples of proteins with a quaternary structure

A

Collagen
Haemoglobin
Catalase

22
Q

What are the two groups for 3D proteins

A

Globular

Fibrous

23
Q

Describe globular proteins

A

Roll up to form ball shaped spherical structures
Soluble in water
Have metabolic roles

Eg haemoglobin

24
Q

Describe fibrous proteins

A
Form fibres (long linear chains)
Repetitive sequence of amino acids
Insoluble in water
Strength and structural roles
Eg keratin
25
What is haemoglobin also referred to as
A conjugated protein
26
What type of protein is haemoglobin
A globular protein with a quaternary structure
27
What does conjugated mean
A protein with a prosthetic group
28
How many polypeptide chains in haemoglobin
Four- 2 alpha 2 beta
29
Name the prosthetic group in each chain and the ion
Haem | Fe2+
30
What type of protein is catalase
Globular
31
What is catalase
An enzyme that speeds up metabolic reactions
32
How many prosthetic groups does haem have
Four
33
What type of protein is insulin
A globular | Transported in blood
34
What type of shape does insulin have
Tertiary
35
The A and B chains in insulin form what - which then form what in the presence of what
Dimer Hexamer Zn2+
36
Keratin | Where is it found and what are the properties
Nails/ horn rhino/ hairs/ skin | Strong/ inflexible/ insoluble
37
Collagen | Where is it found and what are the properties
Walls of arteries/ tendons/ bones/ cartridges Flexible/ long strong rope like
38
Elastin | Where is it found and what are the properties
Walls of arteries- elastic fibres Flexible/ can expand and return to normal size