Exam 1: Chapter 1-4 Flashcards
What are the characteristics of prokaryotes?
-simple cell architecture
-cell wall
-loosely organized genetic information
Define prokaryotes.
Unicellular organism without a nucleus. (bacteria & archaea)
What are the characteristics of eukaryotes?
-linear DNA organization
-membrane bound structures
-prokaryotic relics
Define eukaryotes.
Complex cellular organisms with membrane enclosed organelles that have specialized functions.
Draw the Amine functional group.
Draw the alcohol functional group.
Draw the thiol functional group.
Draw the ether functional group.
Draw the aldehyde functional group.
Draw the ketone functional group.
Draw the carboxylic acid functional group.
Draw the ester functional group.
Draw the amide functional group.
Draw the Imine functional group.
Draw the phosphoric acid ester functional group.
Draw the diphosphoric acid ester functional group.
What is the biological polymer of an amino acid?
Polypeptide
What is the biological polymer of a monosaccharides?
Polysaccharide
What is the biological polymer of a nucleotides?
Nucleic Acid
What biological momomer is this structure?
Amino Acid
How do you identify a monosaccharide structure?
Sugars have a ~1-1 ratio of carbon: oxygen.
What biological monomer is this structure?
Nucleotide
How do identify a lipid structure?
Lipids have a high ration of carbon to oxygen/nitrogen/phosphorus.
What are residues?
A residue is a monomer that has been incorporated into a polymer.
How are monomers linked together to form different macromolecules?
Covalent bonds
What is a polypeptide?
A polymer of amino acids linked together by peptide bonds.
What is a protein?
A protein is a functional unit consisting of one of more polypeptides.
What kind of bond forms a polysaccharide?
Glycosidic bond.
What kind of bond forms nucleic acids?
Phosphodiester bond.
What are the major and minor roles of proteins?
Major Role:
1. Carry out Metabolic Reactions
2. Support Cellular Structures
Minor Role:
1. Store Energy
What are the major and minor roles of nucleic acids?
Major Role:
1. Encode Information
Minor Role:
1. Carry out Metabolic Reactions
2. Support Cellular Structures
What are the major and minor roles of polysaccharides?
Major Role:
1. Store Energy
2. Support Cellular Structures
Minor Role:
1. Encode Information
If DeltaG is <0, then…
A process is ‘spontaneous’ or ‘favorable’ and products are favored
If DeltaG is >0, then…
A process is ‘non-spontaneous’ or ‘unfavorable’ and reactants are favored
What is catabolism?
Breaking down larger molecules
What is anabolism?
Building complex molecules at the expense of energy.
What is a Hydrogen bond?
Hydrogen bonds occur when an H atom in a molecule, bound to O, N, or F is attracted to the lone pairs in another molecule
What is amphipathic molecule?
A molecule with both polar & non-polar regions
What is the hydrophobic effect?
Nonpolar regions cluster together to maximize the entropy of the surrounding water molecules.
What is the order of strength of intermolecular forces?
Covalent bond > ion-ion > H-bonds > dipole-dipole > London dispersion
What is London dispersion forces?
At any given moment the electrons may shift more to one side which can influence the molecule next to it.
What causes a higher boiling point?
Stronger IM forces
What is the equation for pOH?
pOH = -log [OH]
What is the equation for pH using H+ concentration?
pH = - log [H+]
Does a strong acid have a smaller or big Ka value? pKa value?
Strong acids have larger Ka values, and smaller pKa values
What happens to [HA] and [A] if pH is < pKa?
If pH < pKa than [HA] > [A-]
When the pKas are far apart, which one should be used?
The pKa value closest to the solution pH
When do we consider a buffer to be useful?
Within +- 1 pH of its pKa
What is acidosis?
A condition where blood pH is too low
What is alkalosis?
A condition where blood pH is too high.
How do kidneys help maintain blood pH?
Kidneys usually retain HCO3- while eliminating H+ to prevent acidosis
How do lungs help maintain blood pH?
Lungs breathe faster to raise blood pH and slow breathing to lower blood pH.
When should a solution be mostly unprotanated?
When pKa is above the pH.
What is the general structure of a purine and what are the types?
2 rings; Adenine & Guanine
What is a nucleotide?
A nucleoside with one to three phosphates attached.
What is the general structure of a pyrimidine and what are the types?
1 ring; Cytosine, Thymine, & Uracil
What is a nucleoside?
A nitrogenous base attached to a ribose sugar
What is the structure of DNA?
The two DNA strands are antiparallel and the resulting helix is right-handed.
What is the Tm?
Tm is the point where half of the DNA is completely separated
What increases Tm?
Higher GC content
Draw Alanine. What are the abbreviations?
Draw Valine. What are the abbreviations?
Draw Phenylalanine. What are the abbreviations?
Draw Tryptophan. What are the abbreviations?
Draw Leucine. What are the abbreviations?
Draw Isoleucine. What are the abbreviations?
Draw Methionine. What are the abbreviations?
Draw Proline. What are the abbreviations?
Draw Serine. What are the abbreviations?
Draw Threonine. What are the abbreviations?
Draw Tyrosine. What are the abbreviations?
Draw Cystesine. What are the abbreviations?
Draw Asparagine. What are the abbreviations?
Draw Glutamine. What are the abbreviations?
Draw Histidine. What are the abbreviations?
Draw Glycine. What are the abbreviations?
Draw Aspartate. What are the abbreviations?
Draw Glutamate. What are the abbreviations?
Draw Lysine. What are the abbreviations?
Draw Arginine. What are the abbreviations?
How are amino acids linked together?
Peptide bond formation between the N-terminus and C-terminus
Which amino acids are hydrophobic?
Alanine, Valine, Phenylalanine, Tryptophan, Leucine, Isoleucine, Methionine, Proline
What amino acid forms a disulfide bond and through what interaction?
Nearby Cys side chains will form a disulfide bond in an oxidizing environment
What is Ion-Exchange Chromatography?
Separates proteins by containing charged groups that bind to proteins of the opposite charge
How are bound proteins eluted in Ion-Exchange Chromatography?
Increasing salt concentration or by changing the pH of the buffer to alter the charge of the bound proteins
What is Size exclusion chromatography?
Separates proteins based on size by using small pores and channels in the beads that separate proteins by size and can vary in range to change the % of proteins that will explore each channel.
What is affinity chromatography?
Takes advantage of the natural binding properties of a protein or uses an engineered tag in order to make some proteins bind to ligands in a mixture and the rest of the proteins will elute.
What is SDS-PAGE?
Assesses what is in a protein sample by unfolding proteins and putting them in a gel well in order to measure their size.
What is the primary structure of a protein?
The sequence of amino acid residues.
What is the secondary structure of a protein?
The localized conformation of the polypeptide backbone.
What is the tertiary structure of a protein?
The 3D structure of an entire polypeptide, including all of it’s side chains.
What is a quaternary structure of a protein?
The spatial arrangement of polypeptide chains in a protein with multiple subunits.
What are the different types of regular structures that occur within a protein?
Alpha Helices and beta-sheet secondary structure.
What is a domain?
Regions of a polypeptide that fold independently and have their own functions.
