bio sci 93 midterm 1 Exam Questions with Revised Correct Detailed
Answers with Rationales Guaranteed Pass
Terms in this set (129)
● Properties of life: order, regulation, evolutionary adaptation,
energy processing, growth and development, response to the
environment, reproduction.
● Theme of emergent properties: The biosphere → ecosystems →
communities →
Lecture 1 populations → organisms → organs → tissues → cells → organelles →
molecules
● The cell is the basic unit of structure and function and smallest
to perform activities of life. All cells are enclosed by a
membrane and use DNA as genetic information.
● Structure fits function
● Organisms as open systems
● DNA is the basis of inheritance
● Hydrogen bonds: The H atom forms one covalent bond with
another atom in the same molecule where it is present, and a
second weaker bond (the "hydrogen bond") with an atom in
another molecule
● Cohesion: interaction between water molecules → surface tension
Lecture 2 ● Water can make maximum of 4 hydrogen bonds.
● Hydrophilic substances → Affinity for water, hydrophobic
substances → Repel water
● Water can dissociate into a hydrogen ion and a hydroxide ion.
● Buffers: resist change in pH of a solution
● The main buffer in blood is carbonic acid / bicarbonate
, ● Carbon atoms → building blocks of biological molecules (4
valence electrons and can form four covalent bonds)
● Properties of an organic molecule also depend on the chemical
groups attached to the carbon skeleton.
● Chemical groups: hydroxyl, carbonyl, carboxyl, amino,
sulfhydryl, methyl and phosphate
● Dehydration reaction → synthesizing a polymer, Hydrolysis
→ breaking down a polymer
* A carbohydrate is a molecule consisting of carbon, hydrogen
Lecture 3
and oxygen atoms. Examples of it would be sugars, starches
and fiber. Simplest carbohydrates are monosaccharides.
Disaccharide is 2 monosaccharides joined together by glyosidic
linkage (covalent bond). Polysaccharides are Polymers of 100s-
1000s of monosaccharides.
● Lipids (not polymers) are diverse group of
hydrophobic molecules and are in three forms of fats,
phospholipids, and steroids.
● Fats → saturated fats vs unsaturated fats, Phospholipids →
glycerol + two fatty acids + phosphate group + choline,
Steroids → Carbon skeleton with 4 rings and varying
functional groups
● Amino acids (monomers) → polypeptides (polymer of
amino acids in specific sequence) → proteins (one or more
polypeptides with specific 3-D conformation)
● Proteins are all structured from the same set of 20 amino acids.
● Structure of an amino acid contains: amino group, hydrogen,
carboxyl group and an R group (variable side chain). Make sure
you can identify the polar amino acids vs non polar amino acids
Lecture 4
based on their structures.
● Protein folding: - Primary (amino acid sequence) - Secondary
(hydrogen bonding, Alpha helix vs Beta pleated sheets) -
Tertiary structure (overall shape of polypeptide, R group
interactions) - Quaternary structure (Overall protein structure
resulting from combined polypeptides of 2 or more, stabilized
by R group interactions)
● A single change in the primary structure of a protein can have
pleiotropic effects such as different disease or health
, conditions (ex. Sickle cell anemia)
● Damaged or misfolded proteins are actively degraded by proteasome
● Plasma membrane composition: - Lipids (phospholipids which
are the main fabric of membrane that form the bilayer) -
Cholesterol (regulates membrane fluidity) - Proteins
(embedded in bilayer and control the movement of different
Lecture 5
materials inside and outside of the cell) -Carbohydrates
(present on extracellular surface and are mainly responsible
for cell-cell recognition).
● Fluid mosaic model of plasma membrane
● The cell membrane is fluid.
Answers with Rationales Guaranteed Pass
Terms in this set (129)
● Properties of life: order, regulation, evolutionary adaptation,
energy processing, growth and development, response to the
environment, reproduction.
● Theme of emergent properties: The biosphere → ecosystems →
communities →
Lecture 1 populations → organisms → organs → tissues → cells → organelles →
molecules
● The cell is the basic unit of structure and function and smallest
to perform activities of life. All cells are enclosed by a
membrane and use DNA as genetic information.
● Structure fits function
● Organisms as open systems
● DNA is the basis of inheritance
● Hydrogen bonds: The H atom forms one covalent bond with
another atom in the same molecule where it is present, and a
second weaker bond (the "hydrogen bond") with an atom in
another molecule
● Cohesion: interaction between water molecules → surface tension
Lecture 2 ● Water can make maximum of 4 hydrogen bonds.
● Hydrophilic substances → Affinity for water, hydrophobic
substances → Repel water
● Water can dissociate into a hydrogen ion and a hydroxide ion.
● Buffers: resist change in pH of a solution
● The main buffer in blood is carbonic acid / bicarbonate
, ● Carbon atoms → building blocks of biological molecules (4
valence electrons and can form four covalent bonds)
● Properties of an organic molecule also depend on the chemical
groups attached to the carbon skeleton.
● Chemical groups: hydroxyl, carbonyl, carboxyl, amino,
sulfhydryl, methyl and phosphate
● Dehydration reaction → synthesizing a polymer, Hydrolysis
→ breaking down a polymer
* A carbohydrate is a molecule consisting of carbon, hydrogen
Lecture 3
and oxygen atoms. Examples of it would be sugars, starches
and fiber. Simplest carbohydrates are monosaccharides.
Disaccharide is 2 monosaccharides joined together by glyosidic
linkage (covalent bond). Polysaccharides are Polymers of 100s-
1000s of monosaccharides.
● Lipids (not polymers) are diverse group of
hydrophobic molecules and are in three forms of fats,
phospholipids, and steroids.
● Fats → saturated fats vs unsaturated fats, Phospholipids →
glycerol + two fatty acids + phosphate group + choline,
Steroids → Carbon skeleton with 4 rings and varying
functional groups
● Amino acids (monomers) → polypeptides (polymer of
amino acids in specific sequence) → proteins (one or more
polypeptides with specific 3-D conformation)
● Proteins are all structured from the same set of 20 amino acids.
● Structure of an amino acid contains: amino group, hydrogen,
carboxyl group and an R group (variable side chain). Make sure
you can identify the polar amino acids vs non polar amino acids
Lecture 4
based on their structures.
● Protein folding: - Primary (amino acid sequence) - Secondary
(hydrogen bonding, Alpha helix vs Beta pleated sheets) -
Tertiary structure (overall shape of polypeptide, R group
interactions) - Quaternary structure (Overall protein structure
resulting from combined polypeptides of 2 or more, stabilized
by R group interactions)
● A single change in the primary structure of a protein can have
pleiotropic effects such as different disease or health
, conditions (ex. Sickle cell anemia)
● Damaged or misfolded proteins are actively degraded by proteasome
● Plasma membrane composition: - Lipids (phospholipids which
are the main fabric of membrane that form the bilayer) -
Cholesterol (regulates membrane fluidity) - Proteins
(embedded in bilayer and control the movement of different
Lecture 5
materials inside and outside of the cell) -Carbohydrates
(present on extracellular surface and are mainly responsible
for cell-cell recognition).
● Fluid mosaic model of plasma membrane
● The cell membrane is fluid.
