Amino Acids
The traditional start codon's A.A (Drawing required)
What is methionine?
An enzyme's ability
What is a stabilized and energetically lower transition state?
Polymers of amino acids
What is protein?
These nucleotides form hydrogen bonds with each other
What is A=T, A=U, and G≡C?
Henderson-Hasselbach Equation
What is pH=Pka+log([A-]/[HA])?
110 Da
What is the average weight of an A.A?
2 modes of regulation for enzymes
What is bioavailability and catalytic efficiency?
What is a heterotrimer?
These 4 things are the essential roles of nucleotides
What are...
1 - Energy currency
2 - Intracellular signalling
3 - Structural components
4 - Basic building blocks of nucleic acids
This fold is seen associating with ATP
Beta-Alpha-Beta fold, aka Rossmann fold (Motif)
PH carries no net charge here
What is the isoelectric point (PI)?
The original enzyme substrate binding model vs the currently accepted model
What is the lock and key model vs the induced fit model?
Classes of 3° structure
What are alpha helices, beta sheets, alpha/beta and alpha + beta?
The bond name that links base to the ribose
What is an N-Beta-glycosyl bond?
Beta turn with a carbonyl pointed inwards
What is a type I Beta Turn?
These 6 letters don't have A.A associated with our course or at all (2 are not associated with this course, 4 don't have any)
Names for cofactor groups
What are co-enzymes (organic components) and prosthetic groups (permanently associated)?
Notable mentions since I am unsure if they are considered groups but are types of cofactors: Metal-activated enzyme (loosely bound metal ions) and metalloenzyme (tightly bound metal ion(s))
A condensation reaction between a carboxylic acid and an amine group, which is considered unfavorable
What is a peptide bond?
How a beta-furanose is formed out of a ribose
What forms from a C4 located OH attacking C1 in a ribose?
These molecular interactions are ranked from strong to weak
What is covalent, electrostatic, h-bonds, dipole-dipole, and van deer waals?
The amino acids with A.A Pkas different to the amine group and carbonyl.
What are cystine, aspartate, glutamate, histidine, lysine, arginine, and tyrosine?
3 ways enzymes increase reaction rates in a cell
#1 - Lowering activation energy by stabalizing the transition state
#2 - Providing an alternate path for product formation
#3 - By orienting substrates properly for the reaction to occur
These non-covalent weak interactions are involved in biomolecule complex formation
What are hydrophobic forces, electrostatics, h-bonds, and van der waals?
Reason why RNA is less stable than DNA
Hard to phrase as a question...
#1 - Excess BME + 8.0M urea = denatured. Removed the agents and its renatured.
#2 - Denatured enzyme start. Remove BME first, then UREA. Results in scrambled enzyme.
#3 - Scrambled enzyme start. Add trace amounts of BME. Aqquire native enzyme.
(Proves primary sequence dictates the polypeptide backbone folding into a stable 3D structure)