DNA/RNA Structure
Components of a nucleotide.
Phosphate group, five carbon sugar (ribose or deoxyribose), and a nitrogenous base.
Pre-existing strands act as templates for new strands.
What is semi-conservative replication?
What proteins are made up of.
What are amino acids?
Name the two types of metabolic pathways
Chain
Cycles
What information structure is used to make polypeptides?
What is mRNA?
Type (and number) of bonds between nitrogenous base pairs.
Hydrogen bonds - 2 between Adenine and Thymine, 3 between Guanine and Cytosine.
Enzymes responsible for unwinding and reducing supercoiling at the beginning of DNA replication.
What are helicase and gyrase?
Name of the bond between amino acids and the process that forms these bonds.
Peptide bonds and dehydration synthesis
How do enzymes work when interacting with substrates?
The enzyme causes the substrate to destabilize and undergo chemical stress between the subunits bonds. This is caused by specific reactions that take place between the substrate and the enzyme when placed into the active site.
Three key steps in a polymerase chain reaction.
Denaturation, Annealing, Elongation
Chargaff's Rule
Purines = Pyrimidines or A+G = C+T
What is DNA ligase used for?*
Splicing Okazaki fragments to make a continuous strand.
Name five functions of proteins.
Transport
Hormones
Enzymes
Immunity
Sensation/Response
Movement
Structure
Where does the end-product of metabolic pathways bind to stop the reaction from continuing?
The allosteric site.
Three types of RNA and their functions.
- tRNA - transfer RNA - carries amino acids to the ribosome for synthesis
- mRNA - messenger RNA - transcript copy of the gene which encodes for specific polypeptides
- rRNA - ribosomal RNA - responsible for catalytic activity in the ribosome
Name two differences between a DNA nucleotide and an RNA nucleotide.
1. Ribose vs. Deoxyribose - OH vs. H on carbon
2. Uracil vs. Thymine
Production of RNA sequences from a DNA template
What is transcription?
Define zwitterion.
A molecule that contains both positively and negatively charged functional groups, with the net charge of the entire molecule being neutral (zero).
Describe a non-competitive inhibition graph.
The rate of reaction plateaus as the substrate concentration increases.
Difference between exergonic and endergonic enzymatic reactions.
Exergonic reactions release energy as bonds are broken while endergonic reactions use a lot of energy to build up bonds between molecules.
The covalent bond between two nucleotides, specifically the 3' carbon of one nucleotide and the 5' carbon of the other.
What is a phosphodiester bond?
Most common enzyme used in PCR amplification AND its origin.
What is Taq Polymerase?
Origin: Thermophilic bacterium or Thermus aquaticus
How many proteins are in a proteasome?
Over 1 million proteins.
Difference between competitive and non-competitive inhibitors.
Competitive inhibitors bind on the active site while non competitive inhibitors bind on any other place on the enzyme and change the shape of the enzyme.
[X] has been produced using recombinant gene transfer. [Y], a [Z] bacteria, is cultured and fermented to produce [X].
X = Human insulin
Y = E. coli
Z = Transgenic