4 - Protein Structure Flashcards

1
Q

What are some of the roles of proteins?

A
  • Ligands
  • Receptors
  • Membrane transport
  • Catalysts
  • Muscle contraction
  • Structural support
  • Immune protection
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2
Q

What are the 1,2,3,4 structures of proteins?

A

1 - Covalently bound linear amino acid sequence coded for by a gene

2 - Local arrangement of polypeptide backbone. Hydrogen bonds so alpha helix or beta pleated sheets

3 - 3D spatial arrangement of amino acids, electrostatic attractions, disulphide bonds, VDW

4 - Association of different polypeptides to form a multisubunit protein, all of the above forces

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3
Q

What is the structure of an amino acid?

A
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4
Q

What deermines the properties of an amino acid?

A

The R group

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5
Q

What is an amino acid residue?

A
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6
Q

What can amino acids be classified as?

A
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7
Q

What is pK?

A
  • Measure of acid strength worked out from Ka
  • Smaller pK means greater acid strength
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8
Q

What will happen if:

  1. pH < pK?
  2. pH > pK?
A
  1. Amino acid will be protonated
  2. Amino acid will be deprotonated
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9
Q

What is a conjugate protein?

A

Polypeptide containing a covalent attachment of a non-polypeptide e.g lipoprotein

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10
Q

How is a peptide bond formed and draw a peptide bond?

A
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11
Q

What are the characterisitcs of a peptide bond?

A

- Rigid (N-C has partial double bond characteristics)

- Planar (Ca-CO-NH-Ca all in same plane)

- Trans (Ca‘S on opposite sides)

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12
Q

Why are peptide bonds not cis?

A

Would be steric clashes between R groups as they are too close

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13
Q

What is pI?

A

The isoelectric point of a protein, where there is no overall net charge on the protein

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14
Q

What is the pI of a basic and acidic amino acid?

A

Basic- pI > 7

Acidic - pI < 7

pH > pI deprotonated

pH < pI protonated

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15
Q

What are the differences in structure between alpha helix and beta pleated sheet?

A
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16
Q

What structure of beta pleated sheets isn’t as stable?

A
  • Parallel
17
Q

What are the differences between fibrous and globular proteins?

A

Globular have motifs and domains

18
Q

What is a motif and a domain?

A
  • In globular proteins

Motif: Folding patterned containing multiple secondary structures

Domain: Part of a polpeptide that folds into a distinct shap for a function

19
Q

How do water soluble proteins and membrane proteins fold? fold?

A

Water soluble: Hydrophilic outside, hydrophobic inside

Membrane protein: Reverse

20
Q

What is the main difference between a secretory protein and an intrinsic protein?

A

Secretory protein has disulphide bonds

21
Q

What are all the types of bonds in each protein structure

A
22
Q

How do proteins fold?

A
  • In a semi-ordered process according to the primary sequence
  • Driven by localised folding to find the most stable conformation
23
Q

What are amyloid fibres?

A

Misfolded beta pleated sheet proteins so proteins that were normally soluble are now insoluble

e.g CJD, BSE, dementia

24
Q

How do you work out the ratio of protonated to deprotonated forms of amino acid at a certain pH?

A

Henderson-Hasselbalch