Bio/Biochem Flashcards
What TYPE of Amino Acids will be hydrophilic?
Those with a charge Basic AA (hist, arg, lys) Acidic AA ( Glutamate, apartate) Asparagine and glutamine
What are the four hydrophobic AA?
Alanine, isoleucine, valine, phenylalanine Those with long alkyl chains
Which direction does kinesins travel?
toward the positive end of microtubules
What direction do dyneins travel?
Towards the negative end
Tubulin is polar and has negative and positive sides, where does each connect in mitosis?
Negative at centriole Positive at centrosome
What’s the main difference between coenzymes and cofactors?
Coenzymes are organic materials (like vitamins) Cofactors are inorganic materials (like metals)
What are the water soluble vitamins?
B and C
What is a haloenzyme?
Has all coenzymes/cofactors to get job done
What is an apoenzyme?
Does not have coenzymes or cofactors to get job done
In michaelis mendal kinetics if the Km is high, what is the affinity of the substrate?
Low
Tertiary protein structures are held together mostly by what?
hydrophobic and hydrophilicity
What are cadherins?
glycoproteins that hold similar cell types together by calcium mediated adhesion
What are integrins?
Binding tag that bind to extracellular matrix
What are selectins?
They are very SELECTIVE in that they will only bind to carbohydrate molecules from other cells.
What kind of molecules are impermeable to the cell? (3)
Large Polar Charged
In G protein-coupled receptors what does Gs do?
Stimulates adenylate cyclase, which increases cAMP
In G protein-coupled receptors what does Gi do?
Inhiibits adenylate cyclase, which decreases cAMP
In G protein-coupled receptors what does Gq do?
it activates phospholipase C
Zymogens are what? how are they named?
Inactive enzymes with -ogen
Native page electrophoresis can best compare..?
molecular size or charge
SDS page separates by?
Mass
Isoelectric focusing separates by?
pI
In size-exclusion chromatography what size molecules are slowed down?
Small
How does ion-exchange chromatograhphy work?
the beads are coated with a charge and slow the opposite charge down
What is edman degradation used for?
To cleave and analyze small proteins, 50 to 70 AA
What is the Bradford reagent used for?
It turns blue the more protein you have
Nucleosides are missing what?
phosphate group
What molecule (during DNA replication) is responsible for relieving the tension from supercoiling?
DNA gyrase or DNA topoisomerase II
DNA polymerase reads in what direction? synthesizes in what direction?
3’ to 5’ 5’ to 3’
Proteins are __ to __, DNA is __ to __
N to C 5 to 3
Pneumonic to remember the stop codons
UAA - you are annoying UGA - you go away UAG - you are gone
What does aliphatic mean?
Non-aromatic
What is lactose made up of??
Glucose and galactose
Which is easier to degrade, alpha helical or beta sheets?
alpha helical. This makes it more soluble
Competitive inhibition does what to Km and Vmax?
Km increases Vmax stays the same Affinity changes but saturation stays the same value. Inhibitor binds to the active site because you can outcompete the inhibitor
Noncompetitive inhibition does what to Km and Vmax?
Km stays constant Vmax changes The affinity stays the same but because the noncompetitive attacks the allosteric site the max saturation is effected
To find the isoelectric point of a neutral AA do what? acidic AA? basic AA?
Add the top and lowest pka divide by two Add the bottom two pka divide by two Add the top two pka’s divide by two
anode/cathode: Anions (A-) are attracted to ______ and Cations (A+) are attracted to the ________
anode cathode
What is the difference between an epimer and and an anomer? Both are diastereomers
Epimers differ in chirality at one carbon Anomers differ in chirality at the anomeric carbon ( the carbon that connects a straight chain glucose to a ring glucose)
Structure of glucose
CHO | H - OH | HO- H | H - OH | H - OH | CH2OH
