Study guide 1 (pt 5) Flashcards
How many peptide bonds are formed in an oligopeptide of 4 amino acids?
3
How many water molecules are formed in the formation of 3 peptide bonds?
3
State the function of enzymatic catalysts
speed up reactions
A protein is a
biologically functional molecule made up of one more polypeptides
amino group, carboxyl group, alpha carbon and ‘R’ group.
H
I
NH4+ - C - COO-
I
R groupThere are _________ different amino acids in proteins
20
Which amino acids below will have an R group that is electrically charged at physiological pH?
serine, lysine, glutamic acid
Discuss how only 20 amino acids can be used to form a huge range of polypeptides.
they can be arranged in different combinations
The _________________ of amino acids determines primary structure of a protein
peptide bonds
bonds in secondary structure
hydrogen bonds
The union of _____________ or more polypeptides forms the _______________ structure.
two; quartinary
What molecule found in the nucleus determines the primary structure of a protein
sequence of DNA
Distinguish between the alpha helix and the beta-pleated sheet. What bond is responsible for these two structures?
alpha helix is coiled, beta pleated is straight
hydrogen bonds
List three types of non-covalent intermolecular forces that contribute to the tertiary structure of a protein.
hydrogen bonds, ionic bonds, hydrophobic interaction
Draw the disulfide bridge found in tertiary structure.
S-S
Define denaturation and explain how changes in pH and temperature lead to denaturation of proteins.
changes can cause the bonds to break and unfold the structure
What bonds are notbroken in denaturation, even in irreversible denaturation?
peptide bonds
