BIO 311C FINAL EXAM QUESTIONS AND ANSWERS
A+ GRADED
Define monomers, polymers and macromolecules
What reactions happen in condensation synthesis and hydrolysis?
1) condensation synthesis: MAKES polymers by releasing water molecules,
condensation synthesis is important in anabolic processes (builds complex from simple)
2) hydrolysis BREAKS DOWN polymers into monomers by adding -H to one molecule
and -OH to another (uses n-1 water molecules) while hydrolysis is important in catabolic
processes (breaks down complex into simple)
How are the carbohydrates classified? Know examples of mono- di- and
polysaccharides(storage and structural)
What are the properties and examples of mono-, di- and polysaccharides and
their functions
What are the different kinds of lipids, their properties and their functions
carotenoid
sterol
What are the differences between saturated and unsaturated fats in terms of
structure and function?
Be able to recognize the monomers of carbohydrates, various types of lipids,
amino acids (as polar or non-polar side chain) and nucleotides
Describe the 3D structure of proteins and the bonds that are important at various
levels of 3D structure
primary: amino acid sequence stabilized by peptide bonds
secondary: regular, repeated patterns of folding the polypeptide, stabilized by H-bonds
between the -C=O group of one amino acid and the -NH group of another along the
polypeptide backbone (alpha-helix and B-pleated sheet structures)
tertiary: formed due to irregular bonding between the side chains of amino acids within a
protein
quartenary: interaction of 2+ polypeptides or subunits of multimeric proteins; has H-
bonding, hydrophobic interaction, & disulfide bridges
What happens if a protein or DNA is exposed to increasing temperature or pH?
What are the differences between DNA and RNA in terms of their composition,
structure and functions?
Be able to understand the primary, secondary and tertiary structures of
molecules and understand how their structure relates to their function
Know the names of specific covalent bonds connecting the monomers in each
group
Trace the pathway of proteins as they are synthesized, modified, sorted out and
shipped to various organelles
, Develop practical application of the knowledge about cell wall components in
various organisms.
Relate the structures and functions of cytoskeleton elements in terms of the cell
movements and vesicle transport
Compare and contrast eukaryotic cell structures such as chloroplast and
mitochondrion or smooth ER and rough ER
Connect the various cell parts in terms of their functions or flow of information or
membranes.
Understand how the surface area to volume ratio in a cube-shape cells change
with increase in volume, and speculate how the large cells compensate for the
loss of surface area
Compare and contrast prokaryotic and eukaryotic cells
Compare and contrast plant and animal cells
Develop a logical sequence of events in a cell fractionation and the methods to
separate carbs, lipids, proteins and nucleic acids
List the appropriate methods of microscopy, centrifugation, gel electrophoresis,
chromatography and other techniques to study the structure and function of cells
and molecules depending on the purpose of the experiment
Define metabolism, anabolism and catabolism and give examples for each.
Describe how the two laws of thermodynamics apply to biological systems with
examples
Define entropy, enthalpy and free energy and give examples. Understand how
they are related to each other in the free energy equation
Know examples of exergonic, endergonic, exothermic and endothermic reactions
and combinations of the same
Understand and practice how Keq is calculated with given concentrations of
reactants and products
Describe enzymes and how do they help in a biochemical reaction
What is ATP and how it is used to drive endergonic processes though energy
coupling
Know the relationship between the enzyme active site, free energy and activation
energy changes
Know the different factors affecting enzyme activity and examples
Understand the substrate concentration, competitive inhibitors, non-competitive
inhibitors affect enzyme activity. Know how these inhibitors affect the Vmax and
Km
Understand how allosteric, feedback and chemical modification regulate enzyme
activity
The shortening of telomeres is prevented by
telomerase
According to Gregor Mendel's view of genetics gene is a / an
unit of heredity for a specific trait
In certain plants, tall is dominant to short trait. If a heterozygous plant is crossed
with another heterozygous (tall) plant, what is the probability that the offspring
will be short
1/4
A+ GRADED
Define monomers, polymers and macromolecules
What reactions happen in condensation synthesis and hydrolysis?
1) condensation synthesis: MAKES polymers by releasing water molecules,
condensation synthesis is important in anabolic processes (builds complex from simple)
2) hydrolysis BREAKS DOWN polymers into monomers by adding -H to one molecule
and -OH to another (uses n-1 water molecules) while hydrolysis is important in catabolic
processes (breaks down complex into simple)
How are the carbohydrates classified? Know examples of mono- di- and
polysaccharides(storage and structural)
What are the properties and examples of mono-, di- and polysaccharides and
their functions
What are the different kinds of lipids, their properties and their functions
carotenoid
sterol
What are the differences between saturated and unsaturated fats in terms of
structure and function?
Be able to recognize the monomers of carbohydrates, various types of lipids,
amino acids (as polar or non-polar side chain) and nucleotides
Describe the 3D structure of proteins and the bonds that are important at various
levels of 3D structure
primary: amino acid sequence stabilized by peptide bonds
secondary: regular, repeated patterns of folding the polypeptide, stabilized by H-bonds
between the -C=O group of one amino acid and the -NH group of another along the
polypeptide backbone (alpha-helix and B-pleated sheet structures)
tertiary: formed due to irregular bonding between the side chains of amino acids within a
protein
quartenary: interaction of 2+ polypeptides or subunits of multimeric proteins; has H-
bonding, hydrophobic interaction, & disulfide bridges
What happens if a protein or DNA is exposed to increasing temperature or pH?
What are the differences between DNA and RNA in terms of their composition,
structure and functions?
Be able to understand the primary, secondary and tertiary structures of
molecules and understand how their structure relates to their function
Know the names of specific covalent bonds connecting the monomers in each
group
Trace the pathway of proteins as they are synthesized, modified, sorted out and
shipped to various organelles
, Develop practical application of the knowledge about cell wall components in
various organisms.
Relate the structures and functions of cytoskeleton elements in terms of the cell
movements and vesicle transport
Compare and contrast eukaryotic cell structures such as chloroplast and
mitochondrion or smooth ER and rough ER
Connect the various cell parts in terms of their functions or flow of information or
membranes.
Understand how the surface area to volume ratio in a cube-shape cells change
with increase in volume, and speculate how the large cells compensate for the
loss of surface area
Compare and contrast prokaryotic and eukaryotic cells
Compare and contrast plant and animal cells
Develop a logical sequence of events in a cell fractionation and the methods to
separate carbs, lipids, proteins and nucleic acids
List the appropriate methods of microscopy, centrifugation, gel electrophoresis,
chromatography and other techniques to study the structure and function of cells
and molecules depending on the purpose of the experiment
Define metabolism, anabolism and catabolism and give examples for each.
Describe how the two laws of thermodynamics apply to biological systems with
examples
Define entropy, enthalpy and free energy and give examples. Understand how
they are related to each other in the free energy equation
Know examples of exergonic, endergonic, exothermic and endothermic reactions
and combinations of the same
Understand and practice how Keq is calculated with given concentrations of
reactants and products
Describe enzymes and how do they help in a biochemical reaction
What is ATP and how it is used to drive endergonic processes though energy
coupling
Know the relationship between the enzyme active site, free energy and activation
energy changes
Know the different factors affecting enzyme activity and examples
Understand the substrate concentration, competitive inhibitors, non-competitive
inhibitors affect enzyme activity. Know how these inhibitors affect the Vmax and
Km
Understand how allosteric, feedback and chemical modification regulate enzyme
activity
The shortening of telomeres is prevented by
telomerase
According to Gregor Mendel's view of genetics gene is a / an
unit of heredity for a specific trait
In certain plants, tall is dominant to short trait. If a heterozygous plant is crossed
with another heterozygous (tall) plant, what is the probability that the offspring
will be short
1/4
