Name the structurally most simple amino acid.
Glycine
The “lock and key” theory of enzymes describes _____.
Enzyme specificity
Name the type of bond that helps form alpha helices.
Hydrogen bond
High heat and low pH can cause this occur, which renders a protein non-functional.
Denaturation
The term used to describe an amino acid at a pH where the protonated and unprotonated forms are equal, giving the molecule a net charge of 0.
Zwitterion
Name the 5 components of an amino acid.
Central carbon
Hydrogen atom
Amino group
Carboxyl group
R-group (side chain)
This enzyme is able to break bonds without using water.
Lyase
Name the type of bond that holds amino acids together.
Peptide bond
Enzymes make reactions occur faster by _____.
Lowering activation energy
Vitamins are essential to organisms because they function as _____.
Coenzymes
A chain of amino acids favors this configuration due to steric hindrance.
Trans
In this type of inhibition the inhibitor can bind equally well to the enzyme whether or not the substrate is bound.
Noncompetitive
The level of structure formed when multiple polypeptide chains come together to form a protein.
Quaternary
Name the class of proteins that regulate the activity of cells and organs and usually travel by blood. (Not all of them are proteins, but many are)
Hormones
Ricin exhibitis its toxicity by inhibiting _____.
Ribosomes
The body preferentially absorbs amino acids in this conformation.
L
Name the enzyme that charges tRNAs.
Name the covalent bond formed when 2 sulfur atoms from 2 amino acids come together.
Disulfide bond
Name the protein found in muscle tissue that contains a heme group that binds oxygen.
Myoglobin
What does the Edman degradation procedure of proteins accomplish?
Removes one AA at a time from the N-terminus
Name the aromatic amino acids.
Tyrosine
Phenylalanine
Tryptophan
The kcat/km of an enzyme tells us _____.
Catalytic efficiency
(How apply an enzyme binds and how quickly it turns over)
Beta sheets are formed when amino acids come together in this configuration.
Alternating hydrophilic and hydrophobic AAs
Name the class of proteins that are insoluble in water, resistant to digestion, and provide support to tissues.
Fibrous proteins
Name the 3 most commonly phosphorylated amino acids.
Serine
Threonine
Tyrosine