2.1.2 M) Levels of Protein Structure Flashcards
Primary protein structure:
sequence of amino acids bonded by covalent peptide bonds
How is the primary structure of a protein formed?
- condensation reacts bonds amino acids together and water molecule(s) is released
- covalent peptide bond between the amino acids
What is the primary structure specific for?
the primary structure us specific for each protein (one alteration in the sequence of amino acids can affect the function of the protein)
What is the secondary protein structure?
- initial folding of the protein
- weak negatively charged nitrogen and oxygen atoms interact with weak positively charger hydrogen atoms to form hydrogen bonds which holds the initial folding in place
What shapes are formed in the secondary structure?
- α-helixshape
- β-pleated sheetshape
Which proteins have a secondary structure?
most fibrous proteins e.g. collagen and keratin
How can the bonds in the secondary structure be broken?
the hydrogen bonds can be broken by high temperatures and pH changes
Diagram of α-helixshape and β-pleated sheetshape
Tertiary protein structure:
- 3D shape formed and held together by 4 bonds
- bonds formed between R groups of amino acids
What bonds are formed in the tertiary protein structure?
- Hydrogen- between strongly polar R groups
- Disulphide bond/bridge- only occurs between 2 sulphurs on 2 R groups (only 3 types of amino acids contain sulphur so bond is rare)
- Ionic - between charged R groups
- Hydrophobic/philic interactions- between non-polar R groups within the interior of proteins
What proteins is the tertiary structure common in?
common in globular proteins
Order of weakest to strongest bonds in tertiary structure:
- H bond
- ionic bond
- disulphide bond/bridge
What does tertiary structure determine?
- A polypeptide chain will fold differently due to the interactions (and hence the bonds that form) betweenR groups
- Each of thetwenty amino acidsthat make up proteins has a uniqueR groupand therefore many different interactions can occur creating a vast range of protein configurations and therefore functions
How can a change in the amino acid sequence result in the formation of a non-functional enzyme?
- change in aa sequence
- leads to change in primary structure
- so dif. order of R groups
- dif. secondary structure - may change hydrogen bonding → H bonds may not form or form in different places
- dif. tertiary structure - R groups in dif. places so tertiary bonds may form differently
- 3D shape is different
- so active site no long complementary to substrate
How is a proteins tertiary structure disrupted when heated to a high temp?
- increase in kinetic E of protein
- protein vibrates/moves more
- hydrophobic/philic / hydrogen / ionic bonds / interactions break
- change in 3D shape/conformation of protein
- denatures enzyme
- active site changes shape and is no longer complementary to substrate
- enzyme stops working