B1.2 Proteins

How many different types of amino acids are there?

20

If there’s nitrogen, what type of macromolecule is it?

protein

two amino acids bonded together

dipeptide

In most cases, where do we get the 9 essential amino acids from?

food

How many essential amino acids are there?

9

What happens if you don’t get the 9 essential amino acids?

malnutritioin

Where can we get the 11 non-essential amino acids?

our body and food

What is the R group?

a variable and the key to protein function

What is the general formula for all amino acids?

carboxyl group, central carbon with R group, amino group

A condensation reaction between two amino acids results in the formation of a what?

peptide bond

What is the bond between two amino acids called?

peptide bond

If there are 20^400 possible amino acid sequences, what does that mean?

the polypeptide has 400 amino acids

proteins in the cells which form the dermis of skin

collagen

peptide hormone responsible for uptake of glucose into cells and reduces glucose concentration in the body

insulin

How many R-groups are hydrophobic with between zero and nine carbon atoms?

9

How many R-groups are hydrophillic?

11

How many R-groups can become charged?

7

How many hydrophilic R-groups are polar but never charged?

4

How many R-groups act as an acid by giving up a proton and becoming negatively charged?

4

How many R-groups act as a base by accepting a proton and becoming positively charged?

3

How many R-groups contain rings?

3

What is the primary structure of protein?

sequence of amino acids

What is the secondary structure of a protein?

local folding

What is the tertiary structure of a protein?

whole molecule folding

What is the quaternary structure?

multiple molecule folding

What holds the folds of the molecule together in the tertiary structure?

disulfide bridges

Can you have a quaternary structure but not a tertiary structure?

yes

What happens to a hydrophobic cell?

it sickles/folds in

What happens to a hydrophilic cell?

no folding

What are the three rules for protein folding?

hydrophobicity, charge, cystein sulfur bridges

Cysteine sulfur bridges form strong bonds with what?

sulfur disulfide bridges