©Themoon EXAM SOLUTIONS
25/11/2024 09:27AM
BIOC 201 Exam and Answers
biomolecules / macromolue - Answers✓✓any molecule present in living organisms
-includes large macromolecules: very large molecule like a protein commonly created by
polymerization of smaller subunits (monomers, typically 1,000 atoms or more: (proteins, carbs,
lipids, nucleic acids). Biomolecules can also be small molecules (primary metabolites
secondary metabolites, natural products)
-most are organic compounds created from (O, C, H, N, some contain phosphorous or sulfur)
SPONCH
-biomolecules exhibit directionality + posses chirality (stereo specific)
-Why are biomolecules composed of SPONCH elements?
-More beneficial for organisms to have mol. with strong or weak bonds?
-Extremely strong covalent bond that must constantly be broken to sustain life? - Answers✓✓-
multiple bonds, mostly carbon
-low atomic weight= stronger covalent bonds
-but organisms are dynamic and weak chem bonds are more easily broken and rearranged to
support life sustaining processes. Need both strong and weak bonds
-Triple bond in nitrogen gas must be fixed/ reduced for use
Proteins/ Nucleic acids/ lipids/ carbs - Answers✓✓Proteins-highly versatile biomolecules
- AA--> AA sequence as a linear polymer--> protein native structure
-can be signal molecules, receptors for signal molecules and enzymes, biological catalysts
NA- made of nucleotides, 2 types:
1- DNA: double helix of polymers made of deoxyribose, phosphate, and 4 bases AGCT
, ©Themoon EXAM SOLUTIONS
25/11/2024 09:27AM
2-RNA: single strand polymer made of ribose, phosphate, and AGCU
L- hydrophobic/philic properties
-form barriers (membranes) that allow compartmentalization
-can be fuel molecules and signal molecules
C- fuels and informational molecules
-glucose is a common carb, stored as glycogen in animals, a branched polymer, important
signal molecules in cell-cell recognition
chemical bonding - Answers✓✓-bond forming: exothermic- energy released
-bond breaking- endothermic- energy needed to be absorbed
covalent/ ionic (electrostatic), H bonds/ van der waals interactions/ hydrophobic interactions
(effect) - Answers✓✓C-strong bond (200-1,000 KJ/mol), electrons shared to form bond
-nonpolar- equal sharing
-polar- unequal sharing creating dipoles
I- (100-1,000 KJ/ mol), high electronegativity difference b/w atoms as one atom strips electrons
away from the other
-E transfer creates ions (charged atoms)
-ionic bonds can be found in salts (NaCl)
-cations=+ (e is lost)
-anions=- ( e gained)
H- relatively weak but abundance makes them important (4-20 KJ/mol)
, ©Themoon EXAM SOLUTIONS
25/11/2024 09:27AM
-H atom covalently bonded to 1 electronegative atom is also attracted to another electronegative
atom (O or N).
-3D structures of many biomolecules and macromol structures are determined by h bonds and
hydrophobic interactions
VW- 0.3-20 KJ/mol, weak interactions from fluctuations in electronic charge around atoms, can
be substantial when summed over many atoms. have to be at optimal distance-Van der waals
contact distance
Hydrophobic interactions- molecules that have mutual fear of water, come together in an
aqueous environment, most important non covalent interactions for proteins in aqueous
environments, come into play at closer distances than ionic interactions
vital properties of water - Answers✓✓-anomalous for a substance of rel low molecular weight
-high BP- liquid at rel high temperatures
-high MP- ice exists- climate stabilization
-large amounts of water in all 3 states of matter
-surface tension- cohesion- important for water transport in plants and blood transport in
animals
-ice less dense than water so lakes dont freeze over completely
-unique physical properties attributed to H bonding, derived from the presnece of dipole/ polar
covalent bonds derived from electronegativity/ molecular shape
Gibbs energy - Answers✓✓-Delta G= change in gibbs free energy, negative spontaneous
-Delta H= change in enthalpy (heat)
-T- temp K, always>0
, ©Themoon EXAM SOLUTIONS
25/11/2024 09:27AM
-Delta S- change of entropy, when + more disorder, when - increased order
H S. G.
- +. - -
+. +. +/- - at high temp
- - +/- - at low temp
+. - +. +
hydrophobic effect - Answers✓✓the aggregation of nonpolar groups in water leads to increase
in entropy owing to the release of water molecules into bulk water
-large increase in entropy of released water molecules makes delta G more negative favoring
the clustering of hydrophobic groups
-membrane formation: phospholipids are amphipathic and exclude H2O, delta S>>0, delta
G<<0
-protein folding:
-each unfolded protein mol adopts unique conformation with high entropy (delta S)
-during protein folding, hydrophobic AA cluster in sequence due to hydrophobic effect
-protein mol are driven toward a common folded structure w minimal entropy, while entropy of
released water molecules is maximized
-entropy of each protein molecule decreases while folding process is spontaneous and
entropically driven due to large increase of entropy of the released water. Delta S>>0 for the
net folding reaction
-other forces like H bond and salt bridges help stabilize final conformation
25/11/2024 09:27AM
BIOC 201 Exam and Answers
biomolecules / macromolue - Answers✓✓any molecule present in living organisms
-includes large macromolecules: very large molecule like a protein commonly created by
polymerization of smaller subunits (monomers, typically 1,000 atoms or more: (proteins, carbs,
lipids, nucleic acids). Biomolecules can also be small molecules (primary metabolites
secondary metabolites, natural products)
-most are organic compounds created from (O, C, H, N, some contain phosphorous or sulfur)
SPONCH
-biomolecules exhibit directionality + posses chirality (stereo specific)
-Why are biomolecules composed of SPONCH elements?
-More beneficial for organisms to have mol. with strong or weak bonds?
-Extremely strong covalent bond that must constantly be broken to sustain life? - Answers✓✓-
multiple bonds, mostly carbon
-low atomic weight= stronger covalent bonds
-but organisms are dynamic and weak chem bonds are more easily broken and rearranged to
support life sustaining processes. Need both strong and weak bonds
-Triple bond in nitrogen gas must be fixed/ reduced for use
Proteins/ Nucleic acids/ lipids/ carbs - Answers✓✓Proteins-highly versatile biomolecules
- AA--> AA sequence as a linear polymer--> protein native structure
-can be signal molecules, receptors for signal molecules and enzymes, biological catalysts
NA- made of nucleotides, 2 types:
1- DNA: double helix of polymers made of deoxyribose, phosphate, and 4 bases AGCT
, ©Themoon EXAM SOLUTIONS
25/11/2024 09:27AM
2-RNA: single strand polymer made of ribose, phosphate, and AGCU
L- hydrophobic/philic properties
-form barriers (membranes) that allow compartmentalization
-can be fuel molecules and signal molecules
C- fuels and informational molecules
-glucose is a common carb, stored as glycogen in animals, a branched polymer, important
signal molecules in cell-cell recognition
chemical bonding - Answers✓✓-bond forming: exothermic- energy released
-bond breaking- endothermic- energy needed to be absorbed
covalent/ ionic (electrostatic), H bonds/ van der waals interactions/ hydrophobic interactions
(effect) - Answers✓✓C-strong bond (200-1,000 KJ/mol), electrons shared to form bond
-nonpolar- equal sharing
-polar- unequal sharing creating dipoles
I- (100-1,000 KJ/ mol), high electronegativity difference b/w atoms as one atom strips electrons
away from the other
-E transfer creates ions (charged atoms)
-ionic bonds can be found in salts (NaCl)
-cations=+ (e is lost)
-anions=- ( e gained)
H- relatively weak but abundance makes them important (4-20 KJ/mol)
, ©Themoon EXAM SOLUTIONS
25/11/2024 09:27AM
-H atom covalently bonded to 1 electronegative atom is also attracted to another electronegative
atom (O or N).
-3D structures of many biomolecules and macromol structures are determined by h bonds and
hydrophobic interactions
VW- 0.3-20 KJ/mol, weak interactions from fluctuations in electronic charge around atoms, can
be substantial when summed over many atoms. have to be at optimal distance-Van der waals
contact distance
Hydrophobic interactions- molecules that have mutual fear of water, come together in an
aqueous environment, most important non covalent interactions for proteins in aqueous
environments, come into play at closer distances than ionic interactions
vital properties of water - Answers✓✓-anomalous for a substance of rel low molecular weight
-high BP- liquid at rel high temperatures
-high MP- ice exists- climate stabilization
-large amounts of water in all 3 states of matter
-surface tension- cohesion- important for water transport in plants and blood transport in
animals
-ice less dense than water so lakes dont freeze over completely
-unique physical properties attributed to H bonding, derived from the presnece of dipole/ polar
covalent bonds derived from electronegativity/ molecular shape
Gibbs energy - Answers✓✓-Delta G= change in gibbs free energy, negative spontaneous
-Delta H= change in enthalpy (heat)
-T- temp K, always>0
, ©Themoon EXAM SOLUTIONS
25/11/2024 09:27AM
-Delta S- change of entropy, when + more disorder, when - increased order
H S. G.
- +. - -
+. +. +/- - at high temp
- - +/- - at low temp
+. - +. +
hydrophobic effect - Answers✓✓the aggregation of nonpolar groups in water leads to increase
in entropy owing to the release of water molecules into bulk water
-large increase in entropy of released water molecules makes delta G more negative favoring
the clustering of hydrophobic groups
-membrane formation: phospholipids are amphipathic and exclude H2O, delta S>>0, delta
G<<0
-protein folding:
-each unfolded protein mol adopts unique conformation with high entropy (delta S)
-during protein folding, hydrophobic AA cluster in sequence due to hydrophobic effect
-protein mol are driven toward a common folded structure w minimal entropy, while entropy of
released water molecules is maximized
-entropy of each protein molecule decreases while folding process is spontaneous and
entropically driven due to large increase of entropy of the released water. Delta S>>0 for the
net folding reaction
-other forces like H bond and salt bridges help stabilize final conformation
