Amino Acids
What amino acids correlate with the letters: Trp, Glu, Ile?
Name the types of bonds that are involved in tertiary folding. Are these covalent or non-covalent?
Non covalent= ionic, hydrophobic effects, hydrogen
Covalent= disulfide bridge
Is the active site mainly polar or nonpolar?
Nonpolar
How does an enzyme work? What matters the most for binding an enzyme to a substrate
Lowers Ea in a reaction. Functional (R) groups
What disease is caused by Beta sheet layers that accumulate and form fibrils or plaques
Huntington's Disease
What amino acids are considered breakers? Which ones are makers?
Proline, Glycine, Alanine, Leucine
Hemoglobin is a __________ protein. It has ____ subunits. In relation to binding with oxygen it has p_______ c_________.
globular; 4; positive cooperativity
How are cofactors or coenzymes used?
Help in the reaction process of an enzyme and substrate
What type of inhibitor increases Km and leaves Vmax unchanged?
Competitive
What is the most common type of anemia and is caused by a lack of something
Iron deficient anemia
How is a disulfide bond formed? What amino acid is used?
oxidation, cysteine
Why are parallel beta sheets less structurally sound than anti-parallel beta sheets?
Parallel sheets have hydrogen bonds that are bent and not as strong. Anti-parallel have straight hydrogen bonds that are stronger.
How is an allosteric enzyme different than normal?
What is the x and y axis on the The Lineweaver Burk plot?
x axis = 1/[Km]
y axis= 1/V
What disease causes vascular problems because of the lack of protein that helps with elasticity?
Ehlers Danlos Syndrome
Give 2 examples of amino acids that might be found on the outer portion of a globular protein.
Polar AA
Ser, Thr, Cys, Gln, Asn
Tyr
What is the most abundant protein found in the body? What type of secondary structure forms this protein? Name the two types of uncommon amino acids that are found in this protein
Collagen; alpha helices; hydroxyproline & hydroxylysine
Give three factors that regulate enzyme activity
What type of enzyme cleaves using water? What type of enzyme moves ions across a membrane?
Hydrolase, Translocase
Why is Mad cow disease so serious?
The infectious proteins work to convert normal proteins into bad ones. They can survive harsh environment of GI tract and travel up SNS to get to brain
How are zwitterions related to the isoelectric point?
at the isoelectric point (pH where amino acid has no charge) the amino acid is a zwitterion and can act as either an acid or base
What is elastin used for? What is the amino acid composition of elastin?
Elastin is used for connective tissue structures like the lungs and bladder. It contains lots of proline and lysine
What is a zymogen and give an example?
Protein that is inactive until a peptide portion is removed. Once removed it is active and this action is nonreversible. Ex is blood clotting factors in blood
Describe what happens to the Lineweaver Burk Plot graph of an uncompetitive inhibitor?
X axis decrease ( move left )
Y axis decrease ( move up)
Explain why primary structure is so important in a protein using sickle cell anemia in your answer
Sickle cell anemia is caused by a single nucleotide change in the 6th position. Structure determines function. Changing the single amino acid makes the later structures change because of the change in bonding abilities