Protein structure (4) Flashcards
Semester 1 year 1
What is the primary structure of a protein?
The linear sequence of amino acids in the polypeptide chain
What does the sequence of a polypeptide have?
Directionality
What is the secondary structure of a protein?
-folding of the polypeptide backbone into regular structures
-structures such as: alpha helix, the beta sheet, turns + loops
-generally stabilised by H bonding between amino acid residues
Describe the alpha helix
-coiled structure held together by H bonds
-right handed (can have left handed, but rare)
-often amphiphilic (amphipathic) - have both hydrophobic + hydrophilic character
Where do the hydrogen bonds form in an alpha helix?
Between the main chain C=O of residue i and the main chain N-H of residue i+4 (every 4th residue)
How many residues are there per turn in an alpha helix, how much rise is there and rotation per residue?
-3.6 residues per turn
-1.5A rise per residue
-100 degrees per rotation
What is the alpha helix terminator?
Proline:
-contains a secondary amine
-doesn’t support the helix geometry
Describe beta sheets
-constructed from 2 or more polypeptides H bonded to each other
-each strand is in a nearly extended conformation
-sheets can be constructed from mixed parallel + antiparallel strands
-contains beta turns
What characteristic can beta sheets have due to certain sequences?
Amphipathic character
Describe beta turns
-compact globular nature of many proteins requires reversal in the direction of polypeptide chains
-H bonds between C=O of i residue + N-H of i+3 residue
Describe the supersecondary structure
-molecules of secondary structural elements can be combined with other secondary structure elements or supersecondary structures
-combined using connecting loops
-forms tertiary structure of proteins
Describe the tertiary structure
-assembly of secondary structure elements into native protein structure
-elements of secondary structure are connected by remaining segments in amino acid sequence
-forms connecting loops
-loops can move, so are useful for function
What is the quaternary structure?
-assembly of polypeptide chain into multi-subunit structures
-subunits usually associate non-covalently
What is the subunit interface constructed from?
-H bonds
-buried hydrophobic residues
-sometimes disulfides
What is haemoglobin?
A tetramer of 2 identical alpha subunits + 2 identical beta subunits - hetero-oligomer