Cell Molecular Exam 1 Flashcards

(37 cards)

1
Q

What are the four main biological macromolecules? What is the individual subunit (monomer) that makes up each?

A

Polysaccharide (monomer: monosaccharides)
Proteins (monomer: amino acids)
Nucleic acids (monomer: nucleotides)
Lipids (monomer: fatty acids).

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2
Q

What is the role of ATP in the cell? How does the ATP molecule store energy?

A

ATP serves as the primary energy currency of the cell.

Storing energy in its high-energy phosphate bonds.

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3
Q

Compare and contrast prokaryotic and eukaryotic cells.

A

Prokaryotic cells are unicellular, lack a nucleus, and have no membrane-bound organelles.

Eukaryotic cells are often multicellular, have a nucleus, and contain membrane-bound organelles.

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4
Q

Identify the cellular organelles and their functions.

A

Key organelles include the nucleus (stores DNA), mitochondria (energy production), endoplasmic reticulum (protein and lipid synthesis), and Golgi apparatus (modifies and packages proteins).

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5
Q

What is a model organism? What model organisms are commonly used in biology research?

A

A model organism is a species extensively studied to understand biological processes.

Common examples: plasmodium, yeast, fruit flies, and mice.

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6
Q

What is meant by molecular complementarity?

A

Molecular complementarity refers to the specific interactions between molecules, such as the binding of substrates to enzymes or the pairing of nucleotides in DNA.

Allows for interactions.

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7
Q

Describe the characteristics of the following chemical bonds. What roles do each play in biological molecules?
Covalent, ionic, hydrogen, Van der Waals, hydrophobic interaction.

A

Covalent bonds (strong, share electrons)

ionic bonds (attraction between charged ions)

hydrogen bonds (weak, between polar molecules)
- stabilizies secondary structures

Van der Waals interactions (weak, due to transient dipoles)
- stabilizies teritary and quaternary structures

hydrophobic interactions (nonpolar molecules avoiding water).
- stabilizies teritary and quaternary structures

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8
Q

Explain the difference between hydrophilic, hydrophobic, and amphipathic molecules.

A

Hydrophilic molecules are water-attracting
Hydrophobic molecules are water-repelling
Amphipathic molecules have both hydrophilic and hydrophobic regions.

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9
Q

Identify the structure of a phospholipid and how phospholipids form cellular membranes.

A

A phospholipid consists of a hydrophilic head and two hydrophobic tails, forming a bilayer in cellular membranes.

The heads are on the outside and the tails are on the inside.

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10
Q

How can you determine whether a chemical reaction is spontaneous?

A

A chemical reaction is spontaneous if it has a negative Gibbs free energy change (ΔG < 0).

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11
Q

How do enzymes increase the rate of chemical reactions?

A

Enzymes increase reaction rates by lowering the activation energy required for the reaction.

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12
Q

Name and describe the four levels of protein structure.

A

Primary (amino acid sequence)
Secondary (alpha helices and beta sheets)
Tertiary (3D folding)
Quaternary (multiple polypeptide chains).

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13
Q

Describe the chemical structure of a polypeptide. What type of bond joins the amino acids? How are the two ends of a polypeptide identified? Which end is synthesized first?

A

A polypeptide is a chain of amino acids linked by peptide bonds. It has an N-terminus (amino end) and a C-terminus (carboxyl end), synthesis N-terminus to C-terminus.

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14
Q

Be able to interpret a free energy diagram, enzyme kinetics graph, Vmax, and Km describing an enzyme-catalyzed reaction.

A

A free energy diagram shows the energy changes during a reaction, while enzyme kinetics graphs plot reaction rate against substrate concentration, with Vmax being the maximum rate and Km being the substrate concentration at half Vmax.

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15
Q

How do chaperones promote proper folding of a protein?

A

Chaperones assist in the folding process by preventing misfolding and aggregation of polypeptides.

They provide an environment for folding to occur.

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16
Q

What is the function of the proteasome?

How does the proteasome recognize its protein targets?

A

The proteasome degrades unneeded or damaged proteins, recognizing targets by ubiquitin tags.

17
Q

How is each of the following methods used to study proteins in the laboratory?
a. SDS-PAGE
b. Two-dimensional gel electrophoresis

A

SDS-PAGE separates proteins based on masses.

Two-dimensional gel electrophoresis separates proteins by both size and charge.

18
Q

What is the central dogma of molecular biology?

A

Genetic information flows from DNA to RNA to protein.

19
Q

What are the differences between DNA and RNA?

A

DNA is double-stranded, contains deoxyribose, and has thymine

RNA is single-stranded, contains ribose, and has uracil. Two OH groups.

20
Q

What does it mean that DNA replication is:
a. Semiconservative?
b. Bidirectional?
c. Both continuous and discontinuous?

A

a. Semiconservative means each new DNA molecule has one old and one new strand.
b. Bidirectional means replication occurs in both directions from the origin.
c. Continuous refers to the leading strand, while discontinuous refers to the lagging strand.

21
Q

Describe the chemical structure of a nucleic acid. What type of bond joins the nucleotides? How are the two ends of a polynucleotide molecule identified? Which end is synthesized first? How are the two strands of a DNA molecule held together?

A

Nucleic acids are composed of nucleotides linked by phosphodiester bonds.

The ends are identified as 5’ and 3’, with synthesis starting at the 5’ end.

The strands are held together by hydrogen bonds between complementary bases.

22
Q

Compare and contrast the two methods of repairing a DNA double strand break.

A

Homologous recombination uses a homologous template for accurate repair.

Non-homologous end joining directly ligates the broken ends, which can lead to errors.

23
Q

What are the three main types of RNA? What is the role of each?

A

Messenger RNA (mRNA, which carries genetic information)
Transfer RNA (tRNA, brings amino acids to ribosomes)
Ribosomal RNA (rRNA, forms the core of ribosome structure and function).

24
Q

What three modifications occur during pre-mRNA processing? What is the purpose of each?

A

Capping (protects mRNA and aids in translation)

Polyadenylation (poly-a tail)

Splicing (removes introns and joins exons).

25
What is meant by the template strand and non-template strand of DNA?
The template strand is the DNA strand used for RNA synthesis Non-template strand (coding strand) has the same sequence as the RNA (except for uracil replacing thymine).
26
Define each of the following and explain how it is used in molecular biology research. a. Cloning vector b. Recombinant DNA c. Restriction enzyme d. cDNA
a. Cloning vector (a DNA molecule used to transfer genetic material) b. Recombinant DNA (DNA formed by combining DNA from different sources) c. Restriction enzyme (an enzyme that cuts DNA at specific sequences) d. cDNA (complementary DNA synthesized from mRNA). Also a reversed copy of mRNA
27
What is a gene?
A gene is a segment of DNA that contains the instructions for synthesizing a specific protein or RNA molecule.
28
Describe the structure of a nucleosome.
A nucleosome consists of a segment of DNA wrapped around a core of histone proteins, forming the basic unit of chromatin. bead and string, euchronatim (open) and hetrochromatin (condensed)
29
How do histone modifications regulate chromatin remodeling? What H3 modifications are associated with condensed chromatin?
Histone modifications, such as methylation and acetylation, influence chromatin structure and gene expression. H3K9 methylation is associated with condensed chromatin. Histone tail modifications control chromatin condensation
30
What three components are required for replication and stable inheritance of a chromosome? How were these identified experimentally?
centromere (for segregation) telomeres (for stability) origins of replication (for initiation). Chromosome painting (FISH)?
31
What is the role of the centromere in chromosome segregation?
Base pairs wrap around it, H3 histone gets wrapped around (CENP-A). Allows for faithful separation. The centromere is the region where spindle fibers attach during cell division, ensuring proper segregation of chromosomes.
32
How does telomerase prevent the shortening of chromosomes?
Telomerase adds repetitive nucleotide sequences to the ends of chromosomes, preventing loss of genetic information during replication.
33
What is a polytene chromosome?
A polytene chromosome is a giant chromosome formed by the replication of DNA without cell division, resulting in multiple copies of the chromosome. Done through DNA amplification.
34
Describe each of the following transposable elements: a. Insertion Sequence (IS) b. DNA transposon c. LTR retrotransposon d. LINEs and SINEs.
a. Insertion Sequence (IS) is a simple transposable element that contains only the genes necessary for its movement. b. DNA transposon can move within the genome by a 'cut and paste' mechanism. c. LTR retrotransposon contains long terminal repeats and moves via an RNA intermediate. d. LINEs (Long Interspersed Nuclear Elements) and SINEs (Short Interspersed Nuclear Elements) are non-LTR retrotransposons that can replicate and insert themselves into new genomic locations.
35
Describe Replication
Replication involves unwinding DNA and synthesizing new strands. - proofread by DNA Polymerase - bidirectional
36
Describe Transcription
Transcription involves synthesizing RNA from a DNA template. - Template DNA is transcribed into a complementary RNA strand by RNA Polymerase Initiation - Polymerase binds to promotor sequence, melts and forms bubble, catalyzes phosphodiester linkage of two initial rNTPs Elongation - 3' to 5' down template strand, melting duplex DNA and adding rNTPs Termination - at the transcription stop site polymerases releases the RNA and leaves the DNA
37
Describe Translation
Translation involves decoding mRNA to synthesize proteins. Initiation - assembly of ribosomes Elongation - a-site to p-site to e-site Termination - releases factor, no more amino acids to add