Primary structure
The specific sequence of amino acids that make up the polypeptide chain
Secondary structure
The 3D structure formed as a result of interactions between amino acids such as alpha helix or beta plated sheet
Tertiary structure
The more specific 3D folding of the secondary structure
Quaternary structure
The 3D arrangement of more than one tertiary polypeptide
What is an amino acid made of
Amino group, carboxyl group, hydrogen and R group
Monomers proteins made of
Amino acids
How do amino acids join
Condensation reaction forming a peptide bond
Bonds in primary structre
Peptide bond
Bonds in secondary structure
Hydrogen
Bonds in tertiary and quaternary structure
Hydrogen, ionic, disulphide
Amino acid structure
Carbon, hydrogen, R group, amino group, carboxylic acid group
What does peptide bond look like
H O
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N— C
Where you find polar R groups on protein
On the surface- hydrohphilic and attracted to water
Where you find non polar R groups on protein
Inside- hydrophobic and repel water
What are the 3 types of protein
Fibrous, globular, conjugated
Conjugated protein
Protein with another prosthetic group associated with their polypeptide chains
Fibrous protein
Polypeptide chains remain elongated
Little or no tertiary structure
Has repetitive sequences of amino acids
Has hydrophobic r groups on outside
Globular protein
Polypeptide chains are folded into spherical shape
Has tertiary structure
Does not have repetitive sequences of amino acids
Has hydrophilic r groups on outside
Overall function onpf fibrous protein
Important structural roles in organisms
Overall function of globular proteins
Important roles in metabolic reactions
Haemoglobin fibrous or globular
Globular
Collagen fibrous or globular
Fibrous
Is haemoglobin quaternary
Yes it has 4 polypeptide chains
Is collagen quaternary
Yes it has 3 polypeptide chains
Is haemoglobin conjugated
Yes it has a haem group
Is collagen conjugated
No
Is haemoglobin soluble
Yes
Is collagen soluble
No
Function of haemoglobin
Binds to oxygen and transports it
Collagen function
Structural strength and support
Polymer
Chain of many single monomers joined together in condensation reaction
How do plants and animals differ in amino acids they make
Plants can make all amino acids, animals only make some and get rest through diet called essential amino acids
Structure of phospholipid
Phosphate, glycerol and 2 fatty acids joined by ester bonds
Properties of phospholipid head
Hydrophilic, polar, soluble and attracts water
Properties of phospholipid tail
Hydrophobic, nonpolar, insoluble and repels water
Properties of cell membranes
Fluidity- gives membrane fluidity
Partially permeable- regulates substances in and out of cell
Flexibility
All parts of cell membrane
Phospholipid bilayer, glycoprotein, glycolipid, proteins, channel proteins, cholesterol
Function of glycoprotein
Role in cellular recognition and immune response
Act as receptors for hormones and neurotransmitters
Stabilise membrane
Function of glycolipid
Acts as surface receptors
Stabilise membrane structure
Function of protein in cell membrane
Role in cell signaling pathways and Stabilise membrane structure
Function of cholesterol in cell membrane
Disturbs close packing of phospholipids
Regulates membrane fluidity
Important for membrane stability
Function of channel protein
Control entry and removal of specifi molecules from a cell
Completely span bilayer