Proteins Flashcards

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1
Q

What are the building blocks for proteins?

A

Amino acids

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2
Q

What are proteins made of?

A

Polymers built from monomers

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3
Q

What are monomers?

A

Amino acids

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4
Q

Do amino acids store excess amino acids for later use like fat and carbohydrates?

A

No

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5
Q

What are proteins essential for?

A

Cell function
Enzymes
Structural
Transport
Movement
Defence
Surface Receptors
Carriers

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6
Q

What are the five basic parts of amino acids?

A
  1. Central carbon - alpha
  2. A hydrogen atom
  3. An amino acid group
  4. A carbonyl group
  5. An R group - side chain
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7
Q

What is different in each amino acid?

A

The R group

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8
Q

What two sterioisomers does amino acids (not glycine) exist as?

A

L-form and D-form

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9
Q

What determines the isometric shape?

A

The distribution of atoms around the central carbon atom

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10
Q

What isomer is amino acids found?

A

L-form

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11
Q

What gives amino acids different physiochemical properties?

A

Different R groups

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12
Q

Can some amino acids ionize to carry negative or positive charges?

A

Yes

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13
Q

Does the polarity of an amino acid influence how it interacts with water?

A

Yes

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14
Q

What is the meaning of polar?

A

Two parts with opposite charges
Water loving
Hydrophilic

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15
Q

What is the meaning of nonpolar?

A

No opposing charges
Water hating
Hydrophobic

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16
Q

What do amino acids (monomers) join together to form?

A

Polymers

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17
Q

What reaction is a molecule of water lost in?

A

A condensation reaction

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18
Q

A peptide bond is the strongest form of what bond?

A

A covalent bond

19
Q

What forms when two amino acids joined together?

A

A dipeptide

20
Q

What forms when many amino acids are joined together?

A

A polypeptide

21
Q

Where does the bond form?

A

Between the carboxy group of one amino acid and the amino group from another amino acid

22
Q

What are the four levels of a protein structure?

A
  1. Primary
  2. Secondary
  3. Tertiary
  4. Quaternary
23
Q

What is the definition of a primary protein structure?

A

The sequence of amino acids, joined by peptide bonds
It is the primary structure of a protein

24
Q

What is a secondary protein structure?

A

An alpha helix
A beta pleated sheet
Random coil
Htydrogen bonding betwenn carbonyl group of one amino acid and amino group of another

25
Q

Where is the secondary protein structure found?

A

Myosin in muscle
Keratin in hair and nails

26
Q

Does large R groups cause the helix to be stable or unstable?

A

Unstable

27
Q

What are some globular protein structures?

A

Myoglobin - iron and oxygen binding protein found in muscle tissue
Haemoglobin - iron and oxygen binding protein in blood
Triose phosphate isomerase - catalyses coversion of triose phosphate isomers
20s proteasome - degrade unneeded or damage proteins by proteolysis

28
Q

Is the beta pleated sheet more extended than the alpha helix?

A

Yes

29
Q

What is made by silkworms and spiders?

A

Silk Fibroin

30
Q

What is formation of silk fibroin?

A

Array of antiparrallel beta pleated sheets
Each beta strand has alterning Glycine and Ala or Ser residues

31
Q

How are beta sheets connected?

A

The beta turn

32
Q

What does the beta turn consist of?

A

Four amino acid residues

33
Q

How is the beta turn stabalised?

A

By hydrogen bonding between Carbonyl oxygen of the first residue and the amide hydrogen of the fourth residue

34
Q

What is also part of the beta turn?

A

Glycine and Proline

35
Q

What is the structure of loops and coils?

A

Disordered and flexible

36
Q

What do coils and loops connect?

A

Secondary structure elements

37
Q

Is there a common pattern in loops and coils?

A

No
Not like beta turns

38
Q

What group are tertiary structures involved in?

A

R groups
Side chains

39
Q

What are valine side chains?

A

Hydrophobic side chains

40
Q

What is an example of hydrogen bonds between groups in side chains?

A

Serine

41
Q

Can ionic charged side chains form ionic bonds?

A

Yes

42
Q

What bonds can sulphur containing grouos form?

A

Covalent bonds

43
Q

What are prions?

A

Misfolded proteins which are found in several fatal neurodivergent diseases