Protien Structure and Function Flashcards
Under what conditions do amino acids act as a base ?
- in low pH
- excess H+
Under what condition do amino acids act as a acid
- excess OH-
- High PH
Describe the structure of the L isomer of amino acids
- 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
Describe the structure of D isomers of amino acids
- When viewed along the hydrogen in the hydrogen-carbon alpha
- CoRN is read in a anti-clockwise direction
- Forms bacterial cell wall
What is the most common conformation of the amino acid side chain R in a polypeptide chain?
Trans is the most common conformation where the R side chain are altering sides along the polypeptide chain
What are peptide residues?
Each repeating unit of the polypeptide is termed a residue. Each residue consists of an invariable unit and a variable R chain - amino acid.
Which conformation of variable regions is less energetically favourable? Cis or Trans
Cis
Describe the structure of a beta pleated sheet?
- 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
Describe the structure of the alpha helix protein structure
- Right handed helix
- Stabilised by hydrogen bonds - H bonds are 4 residues apart
What are 2 important feature os secondary structure proteins ?
- 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
What are tertiary protein structures composed of?
- Combining secondary structures gives rise to tertiary structures - INTRACHAIN
- Many weak chemical bonds sometimes stabilised by covalent bonds
Describe the tertiary structure of proteins
- Globular structure
- Formation depends on interactions of outward facing chains
Describe the quaternary structure of proteins
- 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
Describe the structure of water soluble proteins
- 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