Term
|
Definition
-monomers in peptides and proteins
-energy production |
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|
Term
| How many groups are amino acids arranged into? |
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Definition
|
|
Term
| How are amino acids classified? |
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Definition
|
|
Term
| What are the 20 amino acids coded from? |
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Definition
|
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Term
| What is the source of Nitrogen in Amino Acids? |
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Definition
|
|
Term
| Where do the carbon backbones of amino acids come from? |
|
Definition
| The glycolytic pathway, the pentose phosphate pathway, and the citric acid cycle |
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|
Term
| What are the Non-Polar Amino Acids? |
|
Definition
| Glycine, Alanine, Valine, Leucine, Methionine, and Isoleucine |
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|
Term
| What are the Aromatic amino acids? |
|
Definition
| Phenylalanine, tyrosine, and Tryptophan |
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|
Term
| What are the Polar Amino Acids? |
|
Definition
| Serine, Threonine, Asparagine, Glutamine, Cystine, and Proline |
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|
Term
| What are the Positively charged amino acids? |
|
Definition
| Lysine, Arginine, and histadine |
|
|
Term
| What are the negatively charged amino acids? |
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Definition
|
|
Term
| What is the function of carbohydrates? |
|
Definition
energy production
structure
cellular recognition
signaling |
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|
Term
| What is the cellular function of lipids? |
|
Definition
energy production
membranes
signaling |
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|
Term
| Cellular function of nucleic acids? |
|
Definition
cellular energy
cellular messengers
biological precursors
components of DNA and RNA |
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|
Term
| On what does almost all drug action act? |
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Definition
|
|
Term
| What is the central carbon of an amino acid called? |
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Definition
|
|
Term
| What are the four parts of an amino acid? |
|
Definition
| alpha carbon, hydrogen group, carboxylic acid group and sidechain |
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|
Term
|
Definition
| an acid having both positive and negative charges, but having a total charge of zero |
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|
Term
| What can amino acids act as? |
|
Definition
| can act as an acid or a base |
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|
Term
| What is the structure around the alpha carbon? |
|
Definition
|
|
Term
|
Definition
| lacking an internal plane of symmetry |
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Term
|
Definition
| two forms that are mirror images of each other that can not be superimposed upon one another |
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|
Term
| Are all amino acids chiral? |
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Definition
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|
Term
| When the R group is below the alpha carbon and the amino group is on the left the amino acid is said to be ? |
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Definition
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|
Term
| When the R group is below the alpha carbon and the amino group is on the right the amino acid is said to be? |
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Definition
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|
Term
| In pharmaceutical drugs how many forms of the drug are active? |
|
Definition
|
|
Term
| What what conformation are amino acids in proteins? |
|
Definition
|
|
Term
| why is it important to synthesize a drug with only on chiral conformation? |
|
Definition
| to increase efficacy, and decrease toxicity |
|
|
Term
| How many naturally occuring amino acids are there? |
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Definition
|
|
Term
| what does a small R group indicate? |
|
Definition
| more hydrophilic, and more water soluble |
|
|
Term
| What is the most soluble amino acid? |
|
Definition
|
|
Term
| What is the only cyclic amino acid? |
|
Definition
|
|
Term
| Polar amino acids are more soluble because they ____? |
|
Definition
| can form hydrogen bonds with water |
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|
Term
| Which amino acid forms disulfide bonds? |
|
Definition
|
|
Term
| How many polypeptide chains and disulfide bonds does insulin contain? |
|
Definition
| 2 polypeptide chains and 3 disulfide bonds |
|
|
Term
| why do negatively charged amino acids form salt bridges? |
|
Definition
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|
Term
| Aromatic are groups are _________ and cluster in the protein interior. |
|
Definition
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|
Term
True or False.
Proteins are functional over a large pH range. |
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Definition
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|
Term
| Amino acids in low pH, the COO- ? |
|
Definition
| accepts a proton from water |
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|
Term
| An amino acid at high pH, the NH3+ ? |
|
Definition
| donates a proton to water |
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|
Term
| What is the isoelectric point? |
|
Definition
| the point when the pH of the solution is neutral |
|
|
Term
| how do you calculate the isoelectric point? |
|
Definition
| take the average of the preceeding and proceeding pKa values to the neutral form. (eg -1, 0, +1) |
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|
Term
| What are the titratable parts of an amino acid? |
|
Definition
| carboxylic acid group (COO-), amino group (NH3+) and the side chain |
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|
Term
| What are the least frequently appearing amino acids? |
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Definition
|
|
Term
| What are the most frequently appearing amino acids? |
|
Definition
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|
Term
| What hormone is produced by the pineal gland and regulates the sleep wake cycle? |
|
Definition
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|
Term
| From what amino acid is melatonin derived? |
|
Definition
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|
Term
| Major depression, obsessive compulsive disorder, and other anxiety disorders are associated with? |
|
Definition
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|
Term
| What is the intermediate between tryptophan and melatonin? |
|
Definition
|
|
Term
|
Definition
| A movement disorder that causes involuntary muscle contractions and spasms |
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|
Term
| High levels of serotonin are associated with what disease states? |
|
Definition
| psychosis and schizophrenia |
|
|
Term
| What is epinephrine used to treat? |
|
Definition
|
|
Term
| What reaction forms a peptide bond? |
|
Definition
| A condensation or dehydration reaction |
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|
Term
True or False.
Peptides contain only one free alpha amino group and one free alpha carboxyl group. |
|
Definition
|
|
Term
|
Definition
| phenylketonuia-inability to metabolize phenylalanine |
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|
Term
| What does conjugating glutathione to drugs do? |
|
Definition
| makes them more water soluble |
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|
Term
| Can a protein contain more then one polypeptide chain? |
|
Definition
|
|
Term
| are prostetic groups made up of amino acids? |
|
Definition
|
|
Term
| in what conformation are 99% of peptide bonds? |
|
Definition
|
|
Term
| What two process drive protein folding? |
|
Definition
| burying the hydrophobics and satisfying polar and charged groups |
|
|
Term
| reactions always proceed in the direction of ? |
|
Definition
|
|
Term
| hydrogen bonds and electrostatic interactions contribute to protein structure by? |
|
Definition
| reducing energy cost of unpaired polar/charged groups |
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|
Term
| hydrophobic interactions contribute to protein structure by ? |
|
Definition
| increasing disorder of solvent |
|
|
Term
| how many amino acid residues are required to make one helix turn? |
|
Definition
|
|
Term
| Hydrogen bonds are ______ to the helix backbone? |
|
Definition
|
|
Term
| a repeating unit contains how many residues? |
|
Definition
|
|
Term
| natural proteins are what kind of amino acids? |
|
Definition
|
|
Term
| What are the destabilizing interactions in an alpha helix? |
|
Definition
| Large R groups too close, and electrostatic repulsion |
|
|
Term
| what are stabilizing interactions in alpha helices |
|
Definition
|
|
Term
| how many residues from the end until hydrogen bonding can occur? |
|
Definition
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|
Term
| Helices prefer ____ charged amino acids on the N terminus and _____ charged amino acids on the C terminus end. |
|
Definition
|
|
Term
| two processes in protein folding? |
|
Definition
| nucleation and propogation |
|
|
Term
| What is the first step in protein folding? |
|
Definition
|
|
Term
| Why would glycine disfavor alpha helices? |
|
Definition
| High conformational flexibility when free |
|
|
Term
| Which amino acid most favors the alpha helix? |
|
Definition
|
|
Term
| Which amino acid causes kinks in the helix? |
|
Definition
|
|
Term
| Proline is know as a helix breaker and is one of the ______ that prevents propagation. |
|
Definition
|
|
Term
|
Definition
| hydrogen bonds between adjacent segments of polypeptide chains |
|
|
Term
| Describe parallel beta sheets. |
|
Definition
| Main chain atoms are aligned, and nonlinear N-O/O-H bonds |
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|
Term
| Right handed connections between beta sheets produce _________ angles. |
|
Definition
|
|
Term
| Describe antiparallel beta sheets. |
|
Definition
| N-O/O-H bonds aligned, and main chain atoms are not aligned |
|
|
Term
|
Definition
| 180 degree turns involving four amino acids |
|
|
Term
| how do beta hairpins fold? |
|
Definition
| by beta turn or sidechain stabilization interactions |
|
|
Term
| Which form of proline is always found in beta turns, cis or trans? |
|
Definition
|
|
Term
| What are the two main classifications of proteins? |
|
Definition
|
|
Term
| what do fibrous proteins contribute to the structures they appear in? |
|
Definition
|
|
Term
| Why are fibrous proteins insoluble in water? |
|
Definition
| They contain large amounts of hydrophobic residues |
|
|
Term
| Hair waving and curling is the result of ? |
|
Definition
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|
Term
| What type of helix is collogen? |
|
Definition
|
|
Term
| How many amino acid residues are required to make one turn in collogen? |
|
Definition
|
|
Term
| The amino acid sequence of collogen is generally? |
|
Definition
| A repeating tripeptide unit |
|
|
Term
True or False.
Mutating glycine in collagen can result in lethal diseases. |
|
Definition
|
|
Term
| the interior of globular proteins resemble? |
|
Definition
|
|
Term
|
Definition
| folding pattern involved in two or more secondary structural elements and the connections between them |
|
|
Term
| What is a domain of a protein? |
|
Definition
| part of a polypeptide that is stable or could undergo movement as a single entity with respect to the whole protein |
|
|
Term
| do different domains in a protein have different functions? |
|
Definition
|
|
Term
| What is the quaternary structure of a protein? |
|
Definition
| the 3D arrangement of more then one polypeptide chain |
|
|
Term
| What interactions stabilize protein structure? |
|
Definition
| disulfide bonds, hydrogen bonds, hydrophobic interactions, electrostatics, ion pairs, and van der Waals interactions |
|
|
Term
| What are the two steps involved in peptide synthesis? |
|
Definition
| transcription and translation |
|
|
Term
| What are the three pathways of a protein? |
|
Definition
| folding, aggregation, and recycling by proteases |
|
|
Term
| What contains the information for the 3D folding of a polypeptide |
|
Definition
|
|
Term
| are peptide bonds hydrophillic or hydrophobic? |
|
Definition
|
|
Term
|
Definition
| proteins that facilitate the proper folding of large polypeptides |
|
|
Term
| How do chaperonins function? |
|
Definition
| by bonding to hydrophobic residues preventing inappropriate aggregation |
|
|
Term
| Do chaperonins actively promote folding? |
|
Definition
|
|
Term
| What are two enzymes that promote folding? |
|
Definition
| Protein disulfide isomerase, and peptide prolyl isomerase |
|
|
Term
| What is required for proper protein function? |
|
Definition
| proper folding of the protein |
|
|
Term
| What is the single largest parameter that triggers disease? |
|
Definition
| decrease in protein stability |
|
|
Term
| Decreased protein stability results in? |
|
Definition
| excessive protein aggregation |
|
|
Term
True or False.
Proteins are stable over very narrow experimental perameters. |
|
Definition
|
|
Term
true or false
proteins can be denatured by increasing or decreasing the temperature. |
|
Definition
|
|
Term
| What are the two types of protein aggregates? |
|
Definition
|
|
Term
| are all types of protein aggregates toxic? |
|
Definition
|
|
Term
| what is the lag phase in amyloid formation? |
|
Definition
| nucleation of initial amyloid structure |
|
|
Term
| what is propagation in amyloid formation |
|
Definition
| docking of molecules to the preformed nuclei |
|
|
Term
| What can speed up aggregation? |
|
Definition
| Agitation and agents that destabilize proteins |
|
|
Term
| What is the life span of an RBC in a patient with sickle cell anemia? |
|
Definition
|
|
Term
| how many mutations in hemaglobin cause sickle cell anemia |
|
Definition
|
|
Term
| The result of a mutation on glu-6 results in a hydrophobic/hydrophillic residue? |
|
Definition
|
|
Term
true or false.
sickle cell molecules aggregate forming twinned helical bundles |
|
Definition
|
|
Term
| what factors can denature therapeutic proteins? |
|
Definition
| pH, denaturants, contaminants, pressure, and freezing/thawing |
|
|
Term
| shaking of protein formulations can cause protein aggregation |
|
Definition
|
|
Term
| silicone oil induces protein aggregation |
|
Definition
|
|
Term
| protein aggregates are formed from ? |
|
Definition
| partially unfolded species |
|
|
Term
| first hypothesis in inhibition of aggregates |
|
Definition
| increase stability of native state, while maintaining function and safety |
|
|
Term
| Second hypothesis in inhibition of aggregates. |
|
Definition
| shift equilibrium toward native state |
|
|
Term
| If a ligand binding two states is different, then equilibrium will be shifted to favor state with greater binding |
|
Definition
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