L7 - Introduction to Protein Structure and Function Flashcards

1
Q

List and describe the four levels of protein structure

A
  1. primary
    - The amino acid sequence determined by RNA transcript
  2. secondary
    - Display Alpha helices and beta strands/sheet
  3. tertiary
    - 3D folded protein structure
  4. quaternary
    - Association of multiple folded peptide chains into a larger complex
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2
Q

what is the common structure of amino acids

A

Amino acids consist of an alpha carbon bonded to a carboxyl group (-COOH),
amino group (NH2) and side chain (R-group

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3
Q

what is the common structure of peptide chain

A

Peptide bond formed by dehydration of two residues to form a peptide backbone of one nitrogen group and two carbon groups

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4
Q

types of physical and chemical properties of amino acid side chains

A

Physical properties: Size and Shape

Chemical properties: Charged, uncharged, basic, acidic.

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5
Q

how do the physical and chemical properties influence the folding of the peptide chain

A

the attraction and repulsion of the side chain characteristics to each other form the specialised shapes of proteins as the proteins attempt to pack due to size and shape efficiently.

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6
Q

what interactions determine or stabilise the secondary and tertiary structure

A

Folding is driven by attainment of lowest energy state

Folding determined by hydrophobic effect and stabilised by hydrogen bonding interactions

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7
Q

Describe how primary structure relates to secondary and tertiary structure

A

Primary structure determines the folding of proteins into 2nd and 3rd structures based on the psychical and chemical properties of the AA

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8
Q

Describe how tertiary structure determines the protein function

A
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9
Q

Define a protein domain

A

Are distinct units of a protein that are stably folded independently from the rest of the protein. Domains often confer a particular function or interaction which contributes to the overall function of the protein.

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10
Q
A
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