Bio 340 final Exam - Questions with Verified Answers| Latest Update Graded A+
What are pentoses significant for in cells? They are the sugar component of
deoxyribonucleotides and ribonucleotides.
What do condensation reactions yield as products? Water molecules.
How do proteins change as they move from primary to quaternary structure? They decrease
their Gibbs free energy.
What is the role of enzymes in chemical reactions? Enzymes lower the energy of activation
but do not change the direction of a reaction.
What is an experimental model system? An organism that can be experimentally studied
instead of a more complicated organism.
How is a phospholipid bilayer stabilized? By hydrophobic interactions between
diacylglycerides and polar interactions with water.
What is ATP coupling? It involves covalent linkage of a phosphate to reactants to drive
endothermic reactions.
What are molecular chaperones? Proteins that play a role in the proper folding of other
proteins.
What is a protein domain? A discrete folded region that directs the specific function(s) of a
protein.
Which amino acids are likely positioned in the fatty acid core of the phospholipid bilayer?
Hydrophobic amino acids like phenylalanine.
,What role do covalent bonds play in protein structure? They play a role in tertiary or
quaternary structure formation.
In what environments can phospholipid bilayers, micelles, and liposomes form spontaneously?
In polar or charged environments such as aqueous environments.
What type of bonds can form between cysteine amino acid R groups? Disulfide bonds.
What stabilizes hemoglobin's quaternary structure? Both intramolecular and intermolecular
non-covalent interactions.
What stabilizes secondary structure in proteins? Hydrogen bonds between the amine and
hydroxyl groups of its backbone.
What state are chromosomes in during cell division? They are in their highest state of
packaging and compaction.
What types of bonds are involved in double-stranded DNA? 3 hydrogen bonds between C-G
pairs, 2 hydrogen bonds between A-T pairs, electrostatic interactions, and phosphodiester
covalent bonds.
What are the minimum features needed for a eukaryotic chromosome? Two telomeres,
multiple replication origins, and one centromere.
What does a fluorescent probe signal indicate when added to DNA but not mRNA? It
suggests that Gene A is transcribed into RNA in the cell sample.
What is the difference between pro-insulin and insulin? Pro-insulin has an internal region
that is not present in insulin.
, What does ubiquitylation lead to? The addition of one, multiple, or hundreds of ubiquitin
molecules.
What types of chromatin do chromosomes include in non-dividing cells? Euchromatin and
heterochromatin regions.
Why is heterochromatin not kept tightly packaged all the time? Heterochromatin is too
tightly packaged to be accessible to enzymes and proteins for replication or transcription.
What is a nucleosome composed of? A core histone octamer made up of two subunits of
each H2A, H2B, H3, H4, around 150 base pairs is wrapped.
What is the role of the ATPase subunit in the chromatin remodeling complex? The ATPase
subunit hydrolyzes ATP to generate histone sliding.
What is the structure of Immunoglobulin G (IgG)? IgG is a tetramer that reaches quaternary
structure and is stabilized by both intramolecular and intermolecular disulfide bonds as well as
other non-covalent interactions.
How do enzymes typically act on their substrates? Enzymes bind to their substrate such that
an existing covalent bond within the substrate is strained and breaks at a faster rate.
How do nucleic acids achieve their three-dimensional structures? Like proteins, nucleic acids
achieve three-dimensional structures that direct their interactions and functions.
What is the function of kinases and phosphatases in protein regulation? Kinases add
phosphates and phosphatases remove phosphates to regulate protein folding and hence
protein function.
What are pentoses significant for in cells? They are the sugar component of
deoxyribonucleotides and ribonucleotides.
What do condensation reactions yield as products? Water molecules.
How do proteins change as they move from primary to quaternary structure? They decrease
their Gibbs free energy.
What is the role of enzymes in chemical reactions? Enzymes lower the energy of activation
but do not change the direction of a reaction.
What is an experimental model system? An organism that can be experimentally studied
instead of a more complicated organism.
How is a phospholipid bilayer stabilized? By hydrophobic interactions between
diacylglycerides and polar interactions with water.
What is ATP coupling? It involves covalent linkage of a phosphate to reactants to drive
endothermic reactions.
What are molecular chaperones? Proteins that play a role in the proper folding of other
proteins.
What is a protein domain? A discrete folded region that directs the specific function(s) of a
protein.
Which amino acids are likely positioned in the fatty acid core of the phospholipid bilayer?
Hydrophobic amino acids like phenylalanine.
,What role do covalent bonds play in protein structure? They play a role in tertiary or
quaternary structure formation.
In what environments can phospholipid bilayers, micelles, and liposomes form spontaneously?
In polar or charged environments such as aqueous environments.
What type of bonds can form between cysteine amino acid R groups? Disulfide bonds.
What stabilizes hemoglobin's quaternary structure? Both intramolecular and intermolecular
non-covalent interactions.
What stabilizes secondary structure in proteins? Hydrogen bonds between the amine and
hydroxyl groups of its backbone.
What state are chromosomes in during cell division? They are in their highest state of
packaging and compaction.
What types of bonds are involved in double-stranded DNA? 3 hydrogen bonds between C-G
pairs, 2 hydrogen bonds between A-T pairs, electrostatic interactions, and phosphodiester
covalent bonds.
What are the minimum features needed for a eukaryotic chromosome? Two telomeres,
multiple replication origins, and one centromere.
What does a fluorescent probe signal indicate when added to DNA but not mRNA? It
suggests that Gene A is transcribed into RNA in the cell sample.
What is the difference between pro-insulin and insulin? Pro-insulin has an internal region
that is not present in insulin.
, What does ubiquitylation lead to? The addition of one, multiple, or hundreds of ubiquitin
molecules.
What types of chromatin do chromosomes include in non-dividing cells? Euchromatin and
heterochromatin regions.
Why is heterochromatin not kept tightly packaged all the time? Heterochromatin is too
tightly packaged to be accessible to enzymes and proteins for replication or transcription.
What is a nucleosome composed of? A core histone octamer made up of two subunits of
each H2A, H2B, H3, H4, around 150 base pairs is wrapped.
What is the role of the ATPase subunit in the chromatin remodeling complex? The ATPase
subunit hydrolyzes ATP to generate histone sliding.
What is the structure of Immunoglobulin G (IgG)? IgG is a tetramer that reaches quaternary
structure and is stabilized by both intramolecular and intermolecular disulfide bonds as well as
other non-covalent interactions.
How do enzymes typically act on their substrates? Enzymes bind to their substrate such that
an existing covalent bond within the substrate is strained and breaks at a faster rate.
How do nucleic acids achieve their three-dimensional structures? Like proteins, nucleic acids
achieve three-dimensional structures that direct their interactions and functions.
What is the function of kinases and phosphatases in protein regulation? Kinases add
phosphates and phosphatases remove phosphates to regulate protein folding and hence
protein function.
