Proteins Flashcards

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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
Q

What is haemoglobin also referred to as

A

A conjugated protein

26
Q

What type of protein is haemoglobin

A

A globular protein with a quaternary structure

27
Q

What does conjugated mean

A

A protein with a prosthetic group

28
Q

How many polypeptide chains in haemoglobin

A

Four- 2 alpha 2 beta

29
Q

Name the prosthetic group in each chain and the ion

A

Haem

Fe2+

30
Q

What type of protein is catalase

A

Globular

31
Q

What is catalase

A

An enzyme that speeds up metabolic reactions

32
Q

How many prosthetic groups does haem have

A

Four

33
Q

What type of protein is insulin

A

A globular

Transported in blood

34
Q

What type of shape does insulin have

A

Tertiary

35
Q

The A and B chains in insulin form what - which then form what in the presence of what

A

Dimer
Hexamer
Zn2+

36
Q

Keratin

Where is it found and what are the properties

A

Nails/ horn rhino/ hairs/ skin

Strong/ inflexible/ insoluble

37
Q

Collagen

Where is it found and what are the properties

A

Walls of arteries/ tendons/ bones/ cartridges

Flexible/ long strong rope like

38
Q

Elastin

Where is it found and what are the properties

A

Walls of arteries- elastic fibres

Flexible/ can expand and return to normal size