Proteins Flashcards

1
Q

Proteins

A

Proteins have a variety of functions within all living organisms.
They are very large molecules (polymers) made up of amino acids (monomers)

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2
Q

General structures of an Amino Acids

A
  • The R group is attached to central carbon
  • Each R side chain has a different structure to it
  • There are 20 different types of amino acid
  • It is only the R group which differs in each case
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3
Q

Formation of Polypeptides

A

Can be repeated many times with amino acids being added to produce polypeptide chains which may contain thousands of amino acids
Hydrolysis will break up a polypeptide and release the amino acids. This happens in digestion

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4
Q

Primary structure

A

The sequence of amino acids held with peptide bonds

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5
Q

Secondary structure

A

The folding of the polypeptide chain:
>coiled to form an alpha-helix
>folded to form beta-pleated sheets
-Held with hydrogen bonds

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6
Q

Tertiary structure

A

This is the folding up of the alpha-helix to form a precise three-dimensional shape. Bonds may form between the R groups of the amino acids which find themselves close together. The shape is maintained by 4 types of bonds:

  • hydrogen bonds
  • ionic bonds
  • disulphide bonds
  • hydrophobic bonds
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7
Q

Quaternary structure

A

This is two or more polypeptides held together e.g. insulin has 2 chains, haemoglobin and antibodies have 4
-Held with hydrogen bonds

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8
Q

Fibrous proteins

A

-polypeptide chains don’t fold but remain as straight chains with several chains cross-linked (H bonds)
-secondary structure only - straight chains which can be linked by H bonds (quaternary structure)
-Insoluble
-Very stable and strong
Important for structures and strength e.g.
>tendons, skin - collagen
>hair, beaks, claws - keratin
>silk
>muscle contractile proteins

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9
Q

Globular proteins

A
  • polypeptide chain(s) are highly folded given compact 3D-shape
  • tertiary structure and quaternary structure
  • not very stable; tertiary structure easily disrupted (denatured)
  • Important where precise shapes are required for molecular interactions e.g.
  • enzymes
  • transport proteins - haemoglobin
  • hormones
  • antibodies
  • receptors
  • plasma proteins
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10
Q

Collagen

A

Fibrous protein found in skin and tendons. Provides strength and toughness
Made up of 3 polypeptide chains held with

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