1.4.1: Proteins Flashcards
describe the general structure of an amino acid
amine group, r group, central carbon atom, hydrogen atom, carboxyl group
what is the general formula of an amino acid
NH2CH(R)COOH
what is the R group in an amino acid
variable group
how many different amino acids are there
20
what bond forms when there is a condensation reaction between amino acids
peptide bond
what type of reaction occurs between amino acids to form a peptide bond
condensation reaction
what molecule is removed and from which parts of the amino acids are they removed from a condensation reaction occurs between two amino acids
water is removed - OH from carboxyl group of one amino acid, H atom from amine group of the other amino acid
How can you tell where a polypeptide starts and finishes
start = N terminal (amine group)
end = C terminal (carboxyl group)
Describe what the primary structure of a polypeptide/protein is
number, type and sequence of amino acids in polypeptide chain
what are the bonds in the primary structure of a protein and where are they
peptide bonds between carboxyl group and amine group
Describe what the secondary structure of a polypeptide/protein is
twisting of the primary structure into a regular structure: either alpha helix or beta pleated sheet or both
what are the bonds in the secondary structure of a protein and where are they
hydrogen bonds between carboxyl group and amine group
Describe what the tertiary structure of a polypeptide/protein is
further folding of the secondary structure into a 3D globular shape
what are the bonds in the tertiary structure of a protein and where are they
hydrogen bonds between carboxyl group and amine group
ionic bonds or disulphide bridges between R groups
Describe what the quaternary structure of a polypeptide/protein is
functional protein composed of more than one polypeptide that may be secondary or tertiary in structure but not both
what two types of structure can fibrous proteins have
1 - one secondary polypeptide - functional protein
2 - multiple secondary polypeptides (quaternary structure) - functional protein
what are two structural properties of fibrous proteins
high tensile strength
insoluble
give 2 examples of fibrous proteins and their functions
Collagen - connective tissue e.g. ligaments
Keratin - hard tissue e.g. nails, hair, hooves
what two types of structure can globular proteins have
1- one tertiary polypeptide - functional protein
2 - multiple tertiary polypeptides (quaternary structure) - functional protein
what does the function of a globular protein depend on
function depends on specific 3D shape
what are 2 properties of globular proteins
1 - soluble in water as their surface is hydrophilic and centre is hydrophobic
2 - hydrophobic R groups face inwards, hydrophilic R groups face outwards
What is a conjugated protein and give an example
protein with non polypeptide group e.g. haemoglobin has a haem group
what happens if you change the primary structure of an amino acid
a non functioning protein is produced
what happens when a protein is denatured
change in shape - bonds breaking
what are 2 causes of a protein denaturing and state the bonds that break
high temperature - H bonds break
extreme pH - ionic bonds break
what is the impact on fibrous proteins if it is denatured
lose structural strength
what is the impact on globular proteins if it is denatured
become inactive / insoluble