Protien Structure and Function Flashcards

1
Q

Under what conditions do amino acids act as a base ?

A
  • in low pH

- excess H+

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2
Q

Under what condition do amino acids act as a acid

A
  • excess OH-

- High PH

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3
Q

Describe the structure of the L isomer of amino acids

A
  • When viewed along the hydrogen-carbon alpha bond from the hydrogen CoRN read in a clockwise direction
  • All amino acids incorporated into proteins in living organisms are in L form
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4
Q

Describe the structure of D isomers of amino acids

A
  • When viewed along the hydrogen in the hydrogen-carbon alpha
  • CoRN is read in a anti-clockwise direction
  • Forms bacterial cell wall
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5
Q

What is the most common conformation of the amino acid side chain R in a polypeptide chain?

A

Trans is the most common conformation where the R side chain are altering sides along the polypeptide chain

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6
Q

What are peptide residues?

A

Each repeating unit of the polypeptide is termed a residue. Each residue consists of an invariable unit and a variable R chain - amino acid.

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7
Q

Which conformation of variable regions is less energetically favourable? Cis or Trans

A

Cis

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8
Q

Describe the structure of a beta pleated sheet?

A
  • Secondary protein structure - folding of polypeptides
  • Hydrogen bonds are present between beta strands
  • Parallel or antiparallel arrangement of beta pleated sheets
  • In the parallel arrangement the beta strands are connected together by longer loops
  • In the antiparallel arrangement the beta strand are connected together by short strand Beta-turns
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9
Q

Describe the structure of the alpha helix protein structure

A
  • Right handed helix

- Stabilised by hydrogen bonds - H bonds are 4 residues apart

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10
Q

What are 2 important feature os secondary structure proteins ?

A
  • Arrangement of side chains gives the proteins their protiens their properties and are important for structure and function
  • Side chains protrude outwards from both beta pleated sheets and alpha helix
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11
Q

What are tertiary protein structures composed of?

A
  • Combining secondary structures gives rise to tertiary structures - INTRACHAIN
  • Many weak chemical bonds sometimes stabilised by covalent bonds
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12
Q

Describe the tertiary structure of proteins

A
  • Globular structure

- Formation depends on interactions of outward facing chains

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13
Q

Describe the quaternary structure of proteins

A
  • Made of 2 or more polypeptide chains
  • Same bonds as in tertiary structure but are INTERCHAIN
  • Protein structure may comprise single or multiple subunits
  • Can contain organic or inorganic cofactors
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14
Q

Describe the structure of water soluble proteins

A
  • Hydrophilic residues are mostly on the external surface
  • Hydrophobic residues are mostly on the internal surface
  • Some can assemble into filaments or tubes or coiled coils
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