Protein structure, binding and conformational changes 1.2 Flashcards
What are the 4 animo acid R groups
Basic (positively charged) , acidic (negatively charged), polar and hydrophobic
What gives amino acids their specific shape and properties
The R group
What is a basic amino acid R group
Generally have NH2 which allows them to accept a proton (H+) and become positively charged and strongly hydrophilic as a consequence
What is an acidic amino acid R group
They have a carboxylic acid group which’s allows them to donate a proton, this causes them to become negatively charged and strongly hydrophilic
What are polar amino acid R groups
Hydrophilic as they form weak hydrogen bonds with water molecules. They have a slightly positive and slightly negative side and all have NITROGEN or OXYGEN or SULFUR on their R side chain
What are hydrophobic amino acid R groups
Typical non polar R groups are: hydrocarbons
They do not become charged and cannot form hydrogen bonds with water
What is the primary protein structure
The order in which the amino acids are synthesised during translation into the polypeptide
What bond joins amino acids together
Peptide bond
What reaction forms the peptide bond
Condensation reaction- between OH of COOH and H of NH2
What is the secondary protein structure
Hydrogen bonding along the backbone of the protein strand
What are the secondary protein structure regions called
A-helices, parallel/anti-parallel B pleated sheets, turns
When does the alpha helix occur
Hydrogen bonds form between every fourth peptide bond