Proteins
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What are macromolecules?
-Complex molecules with relatively large molecular mass
What are polymers?
-Are large complex molecule composed of long chains of amino acid
What are monomers?
-Small, basic units
How are polymers formed?
-Condensation reaction- forms a chemical bond between monomers, releasing a molecule of water
How are polymers broken down?
-Hydrolysis reaction- Breaks down chemical bonds between monomers and a water molecule
What are monomers in proteins made from?
-Amino acids
What do 2 amino acid form?
-Dipeptide
What are polypeptide?
-more than 2 amino acid
What are proteins?
• 1/more polypeptides - Are a polymer
What Groups are present in proteins?
• Amino group • Carboxylic group • R group->can form with anything ->determines the tertiary structure
What are the functions of proteins?
• Structural component (e.g. muscle + bone (collagen)) • Enzymes • Hormones • Antibodies • Membrane carriers and pores (e.g. active transport +diffusion)
What bonds do proteins have?
-Peptide bonds to form dipeptides+ polypeptides
What chemical elements are present in proteins?
-Carbon, hydrogen, oxygen, nitrogen and sulphur
How is peptide bonds formed and broken?
• Formed: Condensation reaction + water molecule released - Broken: Hydrolysis reaction+ water molecule add
What are the levels of proteins?
1-Primary structure 2-Secondary structure 3-Teritary structure 4-Quantery structure+
What is a primary structure?
• Sequence of amino acids - Joined by peptide bonds
What is secondary structure?
There are 2 types: • Alpha helix-36 amino acids per 10 turn • Beta pleated- in a flat shape • Have hydrogen bonds
What is the tertiary structure?
• When secondary structure goes through further coiling/ folding • Have bonds- disulfide, ionic, hydrophilic + hydrophobic, Hydrogen
How do the R groups affect the bonds? And how do they bond?
• Some R group attract/ repel • Disulfide bonds-> between cysteine/ S atoms • Ionic bonds-> between oppositely charged R group • Hydrophilic R group on the outside of molecule. Hydrophobic R group on the inside of the molecule • Hydrogen bonds- between delta positive+ negative
What is the quaternary structure?
• Proteins final 3D shape • Made from several different polypeptide chains • Can join with non protein groups->prosthetic groups
Globular proteins
• Have a spherical shape • Hydrophilic R groups on the outside +Hydrophobic R groups on the outside • Soluble in water
What are main globular proteins?
• Hemoglobin • Insulin • Enzymes (e.g pepsin)
What is haemoglobin?
• A conjugated protein (globular protein with prosthetic group) • Transport oxygen+ carbon dioxide • Made of 4 polypeptide chain (quaternary) • Has 2 alpha and beta chains • Soluble • contains haem/ prosthetic group to allow oxygen to be transported
What is insulin?
• Maintains blood glucose concentration • Has 2 polypeptide chains joined together by disulfide bonds • Hydrophilic R group on outside-> dissolve in blood and easily transported • Hydrophobic R group on the inside