proteins

Question 1

proteins

Answer 1

polymers, they have many functions (enzyme, structural, hormones, transport)

Question 2

amino acids

Answer 2

• the monomers that make up proteins
• 20 different kinds that make up proteins in humans
• referred to as 2-amino acids or alpha amino acids. Corboxyl group is on carbon 1 and amino group is on carbon 2
• difference in amino acids are due to R groups/side chains. These can be polar, non polar, acidic, basic

Question 3

peptides

Answer 3

• monomers join together through a condensation reaction to form a peptide (amide functional group)

Question 4

Dipeptide

Answer 4

when 2 amino acids join together through a condensation reaction ( 2 possible products due to different amino and carboxyl groups)

Question 5

tripeptide

Answer 5

when 3 amino acids join together through condensation reaction to form a polymer (more than 50 amino acids in a polymer is a protein)

Question 6

protein structure

Answer 6

• the function of protein is determined by its shape
• all proteins have a primary, secondary, tertiary and quaternary structure

Question 7

primary protein

Answer 7

the specific sequence of amino acids in a peptide chain includes number, type and order

Question 8

secondary

Answer 8

• localised folding of a protein chain due to hydrogen bonding between the oxygen on the carboxyl group of one amino acid and the hydrogen on the other
• influenced by R groups but does not involve interactions of R groups

Question 9

Alpha helix

Answer 9

• molecule coils into a spiral shape due to the hydrogen bond between an oxygen on 1 amino acid and ha ydrogen 4 amino acids down

Question 10

beta pleated sheets

Answer 10

• sections of the peptide chain line up parallel to each other due to hydrogen bonds between 1 amino acid and another on an adjacent part of the chain

Question 11

tertiary

Answer 11

• overall 3D shape of a protein due to different functional groups in the R groups interacting and causing the protein to fold
• interactions between R groups include H bond (NOF), dipole dipole, dispersion, ionic bonds and covalent bond between cysteine R groups

Question 12

quatenary

Answer 12

• 2 or more polypeptide chains interact to produce larger units

Question 13

Enzymes

Answer 13

• Proteins that behave as biological catalysts lower activation energy
• very specific in their structure
• Their function is very dependent on shape, tertiary structure. A change in temperature or pH can denature a protein by interfering with the forces in the tertiary structure =.
  if the protein folds differently, no longer has the correct shape, no longer functions for its specific role