Bio/Biochem Flashcards
Primary alcohols are oxidized to ______
Aldehydes
Secondary alcohols are oxidized into _____
Ketones
If the highest priority group in a molecule is an ester, the suffix of the molecule will be:
-oate
Enamines and imines can interconvert through:
Tautomerization
The aldol reaction produces what?
A molecule with a carbonyl group and an alcohol group
An aldol condensation is a two reaction process that includes what?
An aldol reaction that combines aldehydes/ketones and then a dehydration reaction
Carboxylic acid derivatives include:
Acyl halides, anhydrides, esters, and amides
What is indicative of a transesterification reaction?
An ester reacting with an alcohol using an acid or base
What is the relationship between leaving group stability and atomic radius?
Leaving group stability increases with atomic radius
How does atomic radius change as you go down the periodic table?
Atomic radius increases as you go down the periodic table
What makes a carbon an alpha carbon?
An alpha carbon is the first carbon from the carboxyl group carbon
Name the acidic amino acids
Aspartic acid
Glutamic acid
Name the basic amino acids
Lysine
Arginine
Histidine
What is Histidine’s charge at physiological pH?
Uncharged
What is the charge on acidic amino acids at physiological pH?
-1
What is the charge on basic amino acids at physiological pH?
Arginine and lysine will have a +1 charge
Name all of the amino acids that could hold a charge
Aspartic acid, glutamic acid, histidine, arginine, lysine
Explain the SNoW DRoP Mnemonic
Southern blots look at DNA
Northern blots look at RNA
Western blots look at Protein
What does a low Km mean?
This means that it does not take much substrate to saturate the enzyme, thus indicating a high substrate-enzyme affinity
Explain a competitive inhibitor and its effects on Km and Vmax
The inhibitor molecule is similar enough to the substrate that it can bind to the active site to stop it from binding to the substrate. Km will increase because it takes more substrate to saturate, but Vmax will be unchaged.
Explain a noncompetitive inhibitor and its effects on Km and Vmax
The inhibitor molecule binds to the enzyme at a location other than the active site (an allosteric site). The substrate can still bind to the enzyme, but the inhibitor changes the shape of the enzyme so it is more difficult to catalyze the reaction. Km will remain unchanged because the substrate can still bind, but Vmax will decrease.
Explain a mixed inhibitor and its effects on Km and Vmax
The inhibitor molecule can bind to the enzyme alone or the enzyme-substrate complex, and thus does not prevent the substrate from binding. All mixed inhibitors lower Vmax to some extent, and its effect on Km depends on whether the inhibitor binds like a competitive or uncompetitive inhibitor.
Explain an uncompetitive inhibitor and its effects on Km and Vmax
Uncompetitive inhibitors bind to the enzyme-substrate complex, but the substrate remains bound to the enzyme, thus Km decreases. The substrate stays bound to the enzyme for a longer period of time, so Vmax is lowered as well.
If the highest priority group of a molecule is an aldehyde, what will the suffix be?
-al
In keto-enol tautomerism, which form is favored at equilibrium?
The keto form because the carbonyl bond is stronger than the C-C double bond
Name 3 major functions of the smooth ER?
Cholesterol synthesis
Phospholipid production
Calcium storage
Where does beta oxidation take place in eukaryotic cells?
In peroxisomes
What are gap junctions made of?
Connexin
What do gap junctions allow?
Gap junctions allow for the flow of small molecules and solutes between cells
Which motor protein moves toward the plus end of microtubules?
Dynein
Microfilaments are made up of:
Actin
What is a phosphodiester bond?
A phosphodiester bond is a covalent bond between the oxygen on the 3’ carbon of the first nucleotide and the phosphorus group on the 5’ carbon of the second nucleotide
What is the role of specific transcription factors?
Specific transcription factors bind to response elements to promote or inhibit transcription