BIO302 EXAMINATION TEST 2025/2026 QUESTIONS AND
ANSWERS RATED A+
✔✔microtubule stabilization - ✔✔-microtubule associated proteins (MAPS)
-ex. Tau protein, should bind to microtubule and cause them to be stable, tau gets too
many phosphate groups, can't bind and stabilize, stop communicating.
✔✔microfilaments/actin filaments - ✔✔-G-actin polymerize, form F-actin, strings of actin
protein, not dimer.
-ADP needed at -, + actin bound to ATP
-Polar structure like microtubules
-not hollow, lot thinner than microtublers.
✔✔microfilament structure - ✔✔-motility by crawling
-movement of vesicles
-phagocytosis (creating a vesicle basically)
-white blood cell and bacteria
motor= myosin (5 classes)
✔✔Cytokinesis - ✔✔when cell pinches in two, after mitosis is done
-ring of actin in middle helps with clevage furrow
✔✔myosin - ✔✔-myosin V (+ end only)
-myosin II (both ways)- sliding against actin= muscle contraction
✔✔Intermediate filaments - ✔✔-strengthening and scaffolding
-chemically heterogeneous (each class is chemically different)
-hair and nails, keeps strength
-need to be overlapping for structure
✔✔the endoplasmic reticulum - ✔✔-made of phospholipid bilayer
-lumen or cisternal space, opening in ER, stack of tubes, making protein in rough ER
✔✔polarized structure of a secretory cell - ✔✔organelles one side, cytoplasm w/
vesicles on other side, full of mucus going to be secreted
✔✔signal peptide - ✔✔A sequence of about 20 amino acids at or near the leading
(amino) end of a polypeptide that targets it to the endoplasmic reticulum or other
organelles in a eukaryotic cell.
-SRP binds to this sequence on the ribosome, causes ribosome o stop unless binded to
RER
-SRP falls off after contacting SRPR, signal peptide gets chopped off.
, ✔✔Processing of newly made protein in ER - ✔✔N-term, signal peptide removed w/
signalpetidase
-carbohydrates added by oligo(many)sacchar(sugar)yltransfer(move)ase(enzyme)
-addition of sugars to oligosaccharide by glycosyltransfrases
-glycosulation
✔✔Glycosulation - ✔✔adding sugars to protein, or other molecules
✔✔ERGIC - ✔✔endoplasmic reticulum golgi intermediate compartment
-fusion of vesicles leaving the rough ER, form tube, between rough ER and golgi
✔✔Golgi apparatus cis-face - ✔✔sort from either back to RER or next golgi station
✔✔Golgi apparatus trans-face - ✔✔sorting station to separate proteins into various
types of vesicles depending on their end destination
-GLYCOSYLATION of lipids, proteins, can get additional modifications here
✔✔vesicle types - ✔✔COP-II- coated vesicles: from ER to golgi (anterograde)
COP-I- coated vesicles: from golgi to ER (retrograde)
✔✔vesicle leaving plasma membrane process - ✔✔-RAB protein on vesicle and target
membrane (magnetic almost, recruit tethering proteins)
-V-SNARE on vesicle membrane interacts w/ T-SNARE on target membrane (proteins)
-interaction of snares form
-rise in CA+2 concentration in cell, ATP hydrolysis at membrane, full fusion.
✔✔chemistry of life - ✔✔structure fits function
✔✔covalent bonds - ✔✔sharing of electrons, slightly positive and slightly negative
charges
-polar/nonpolar molecules
TWO TYPES:
-equal sharing, nonpolar
-not equal, polar
(USUALLY C,H,O,N, ORGANIC ATOMS)
Polar: not equal sharing, slightly positive and slightly negative charges
Nonpolar: equal sharing of electrons, equal pull
✔✔noncovalent bonds - ✔✔hydrogen bonds
ionic bonds
hydrophobic and hydrophilic interactions
ANSWERS RATED A+
✔✔microtubule stabilization - ✔✔-microtubule associated proteins (MAPS)
-ex. Tau protein, should bind to microtubule and cause them to be stable, tau gets too
many phosphate groups, can't bind and stabilize, stop communicating.
✔✔microfilaments/actin filaments - ✔✔-G-actin polymerize, form F-actin, strings of actin
protein, not dimer.
-ADP needed at -, + actin bound to ATP
-Polar structure like microtubules
-not hollow, lot thinner than microtublers.
✔✔microfilament structure - ✔✔-motility by crawling
-movement of vesicles
-phagocytosis (creating a vesicle basically)
-white blood cell and bacteria
motor= myosin (5 classes)
✔✔Cytokinesis - ✔✔when cell pinches in two, after mitosis is done
-ring of actin in middle helps with clevage furrow
✔✔myosin - ✔✔-myosin V (+ end only)
-myosin II (both ways)- sliding against actin= muscle contraction
✔✔Intermediate filaments - ✔✔-strengthening and scaffolding
-chemically heterogeneous (each class is chemically different)
-hair and nails, keeps strength
-need to be overlapping for structure
✔✔the endoplasmic reticulum - ✔✔-made of phospholipid bilayer
-lumen or cisternal space, opening in ER, stack of tubes, making protein in rough ER
✔✔polarized structure of a secretory cell - ✔✔organelles one side, cytoplasm w/
vesicles on other side, full of mucus going to be secreted
✔✔signal peptide - ✔✔A sequence of about 20 amino acids at or near the leading
(amino) end of a polypeptide that targets it to the endoplasmic reticulum or other
organelles in a eukaryotic cell.
-SRP binds to this sequence on the ribosome, causes ribosome o stop unless binded to
RER
-SRP falls off after contacting SRPR, signal peptide gets chopped off.
, ✔✔Processing of newly made protein in ER - ✔✔N-term, signal peptide removed w/
signalpetidase
-carbohydrates added by oligo(many)sacchar(sugar)yltransfer(move)ase(enzyme)
-addition of sugars to oligosaccharide by glycosyltransfrases
-glycosulation
✔✔Glycosulation - ✔✔adding sugars to protein, or other molecules
✔✔ERGIC - ✔✔endoplasmic reticulum golgi intermediate compartment
-fusion of vesicles leaving the rough ER, form tube, between rough ER and golgi
✔✔Golgi apparatus cis-face - ✔✔sort from either back to RER or next golgi station
✔✔Golgi apparatus trans-face - ✔✔sorting station to separate proteins into various
types of vesicles depending on their end destination
-GLYCOSYLATION of lipids, proteins, can get additional modifications here
✔✔vesicle types - ✔✔COP-II- coated vesicles: from ER to golgi (anterograde)
COP-I- coated vesicles: from golgi to ER (retrograde)
✔✔vesicle leaving plasma membrane process - ✔✔-RAB protein on vesicle and target
membrane (magnetic almost, recruit tethering proteins)
-V-SNARE on vesicle membrane interacts w/ T-SNARE on target membrane (proteins)
-interaction of snares form
-rise in CA+2 concentration in cell, ATP hydrolysis at membrane, full fusion.
✔✔chemistry of life - ✔✔structure fits function
✔✔covalent bonds - ✔✔sharing of electrons, slightly positive and slightly negative
charges
-polar/nonpolar molecules
TWO TYPES:
-equal sharing, nonpolar
-not equal, polar
(USUALLY C,H,O,N, ORGANIC ATOMS)
Polar: not equal sharing, slightly positive and slightly negative charges
Nonpolar: equal sharing of electrons, equal pull
✔✔noncovalent bonds - ✔✔hydrogen bonds
ionic bonds
hydrophobic and hydrophilic interactions
