Understanding Cell Biology: Structure, Function, and Processes
General Properties and Types of Cells
Cell Theory
- All organisms are made of cells.
- The cell is the fundamental unit of life.
- Cells come from pre-existing cells.
What is a Cell?
- Contains a stable blueprint of information (DNA).
- Has a discrete boundary separating the cell interior from the environment (cell membrane).
- Ability to harness material and energy from the environment.
- Able to read and interpret instructions (DNA).
The Central Dogma of Molecular Biology
- Describes the basic flow of information in a cell.
- Pathway from DNA → Transcription → RNA → Translation → Protein.
Purpose of Cellular Membrane
- Controls the movement of material in and out of the cell.
- Internal membranes divide cells into discrete compartments – each specialized for a particular function (e.g., the nucleus houses DNA).
Why Prokaryotes (Bacteria) are Successful
- Small size.
- Reproduce rapidly.
- Ability to obtain energy from diverse sources.
Why are Bacteria Small Compared to Eukaryotes?
- Small cell = higher surface area to volume ratio.
- Diffusing molecules do not have to travel as far.
Similarities & Differences in Bacteria (Prokaryote) vs. Eukaryote Cell
The Three Domains of Life
Prokaryotes (Bacteria) | Eukaryotes | |
Differences |
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Similarities |
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Bacteria | Archaea | Eukarya |
Lack nucleus | Lack nucleus | Has nucleus |
All single-cell microorganisms | All land plants & animals |
Parts of the Cell
Nucleus
- Stores the cell’s genetic information (DNA).
- Site for RNA synthesis.
Nucleoid
Discrete region of the cell where DNA is concentrated in prokaryotes.
Plasmids
Small circular molecules of DNA that carry additional genes in bacteria.
Plasma/Cell Membrane
- Composed of phospholipids and proteins.
- Regulates material flow in & out of the cell.
Cell Wall
- Only in plants.
- Rigid barrier.
- Composed of polysaccharides.
Mitochondria
Produces most of the ATP (serves as the energy currency of the cell).
Chloroplasts
- Enables plant cells to harness the sun’s energy.
- Synthesizes sugars.
Metabolism
Chemical reactions by which cells convert energy from one form to another.
Transcription
The synthesis of RNA from a DNA template – existing proteins create a copy of DNA’s information via RNA (step 1).
Translation
When specialized molecular structures in the cell “read” the RNA molecule to determine what building blocks to use to create a protein (step 2).
Lipids
Components of Cell Membrane
Made of PHOSPHOLIPIDS → made of:
- Glycerol backbone attached to a phosphate group and 2 fatty acids.
- Phosphate head → polar.
- Fatty acid tails → hydrophobic & no hydrogen bond.
Why Phospholipids Arrange in an Aqueous Environment
Phospholipids are amphipathic = a molecule with both hydrophilic and hydrophobic regions. In water:
- Polar heads go on the outside & interact with water.
- Nonpolar tails go inside away from water.
- Forms LIPOSOME, BILAYER (less bulky head & 2 tails), or MICELLE (bulky head & single tail).
Reasons for Fluid Nature of Membranes
- Extensive van der Waals forces (LDF & DPDP) between fatty acids.
- Can be easily broken & reformed → allow lipids to move within the plane of the membrane → therefore FLUID.
Types of Non-Covalent Interactions Amongst Various Parts of Membrane Components
- Van der Waals forces amongst lipids → break & reform to move along the plane of the membrane.
- Cholesterol (amphipathic attaching to lipid):
- Cholesterol head (hydrophilic OH group) interacts with the hydrophilic phospholipid head.
- Cholesterol ring (hydrophobic) has van der Waals interactions with lipid fatty acid chains.
Factors Affecting Fluidity of Cell Membrane
- Length of fatty acid tail: long fatty acid tail → more van der Waals interactions → tighter packing → reduced lipid mobility & fluidity.
- Presence of double bonds between neighboring carbon atoms: no double bonds → straight & tight packed → reduced mobility.
Role of Cholesterol in Maintaining Membrane Fluidity
- Decrease fluidity in warm/most temperatures: interaction of the rigid ring of cholesterol with the fatty acid tail reduces the mobility of phospholipids (kinks).
- Increase fluidity in low temperatures: cholesterol prevents phospholipids from packing tightly with other phospholipids → prevent transition from fluid to solid-state.
Different Types of Proteins Found in Cell Membrane
- Transporter: Moves ions & other molecules across the membrane.
- Receptor: Allows the cell to receive signals from the environment.
- Enzyme: Catalyzes chemical reactions.
- Anchor: Attaches to other proteins and helps maintain cell structure & shape.
Integral Membrane Protein
PERMANENTLY associated with the cell membrane → cannot separate from the membrane without destroying the membrane (typically transmembrane proteins).
Peripheral Membrane Proteins
TEMPORARILY associated with the lipid bilayer → easily separated from the membrane.
Transmembrane Proteins
(Most integral membrane proteins are this) composed of 3 regions:
- 2 hydrophilic regions on each side of the membrane.
- 1 hydrophobic region through the membrane.
The Fluid Mosaic Model
The idea that lipids & proteins coexist in the membrane and both are able to move in the plane of the membrane.
Membrane Permeability
What Chemical Properties Make the Lipid Bilayer Selectively Permeable?
- Hydrophobic interior of the bilayer: prevents ions, charged, or polar molecules from diffusing across the plasma membrane.
- Packed bilayer: prevents macromolecules (e.g., proteins & polysaccharides) from crossing the membrane alone → too large.
- Gas, lipids, and small polar molecules can freely move across the bilayer.
Diffusion | Facilitated Diffusion | Osmosis | |
Similarities |
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What do they move? | Gases, lipids, small polar molecules | Macromolecules and ions | Water |
How do they move? | Directly through the lipid bilayer | Via channel or carrier (transport protein) | Via aquaporins |
Primary Active Transport | Secondary Active Transport | |
Similarities | Moves molecules against the concentration gradient | |
Energy Source | Directly from ATP | Potential energy of a small ion (proton) from high to low concentration |
Driving Force | Pumps | Electrochemical gradient |
Hydrophobic Effect
It is energetically favorable for a molecule to make the strongest type of intermolecular interaction available – higher entropy molecules can make more arrangements → spontaneous bilayer.
Why Membrane is Necessary as Cell Size Increases
- Not enough surface area: volume ratio to complete cellular reactions (e.g., transport essential nutrients), the membrane = more surface area for diffusion.
- Diffusion travel is long.
- Nutrients/chemicals necessary for reactions are easily diluted in large cells → membrane-bound organelles concentrate diffused solutes in areas.
Ways that Cells Avoid Cell Shrinkage and Lyses (Bursts) When Not in Isotonic Environment
- Contractile Vacuole – compartments that take up excess water from inside the cell then expel it via contraction when hypotonic:
- Take in water by aquaporin.
- Take water with a proton through pumps, with water following by osmosis.
- Cell Wall: Allows turgor pressure to build up → opposes the driving force of water to enter.
- Vacuole: Absorbs water and contributes to turgor pressure.
Proteins
Characteristics of an Amino Acid
- Has a central carbon – called the alpha carbon.
- Covalent bonds to the amino group.
- Covalent bond to the carboxyl group.
- Covalent bond to the R group – AKA side chain.
Covalent Bonds Between Backbone? | Covalent Bonds Between R Groups? | Noncovalent Bonds Between Backbone? | Noncovalent Bonds Between Backbone & R Groups? | Noncovalent Bonds Between R Groups? | |
Primary (Sequence) | Yes | ||||
Secondary (Helix/Sheet) | Yes | ||||
Tertiary (Protein Fold) | Yes (if S-S bonds) | Yes | Yes | Yes | |
Quaternary (2+ Subunits) | Yes (if S-S bonds in cysteine) | Yes | Yes | Yes |
Primary Structure
Peptide bond links α-amino with the next α-carboxyl – the sequence of amino acids in a protein (primary) determines how a protein folds.
Secondary Structures Result from Hydrogen Bonds
- α-helix: Polypeptide backbone is twisted tight in a RIGHT-handed coil → 3.6 amino acids per complete turn → helix is stabilized by hydrogen bonds between carbonyl & amide groups → R groups project out which DETERMINE where the α-helix is located in the protein.
- β-sheet: Polypeptide folds back and forth on itself → forming a PLEATED sheet → R groups project alternately above & below the plane of the β-sheet → 4 to 10 polypeptide chains side by side → amides in each chain are hydrogen-bonded to the carbonyls on either side.
Tertiary Structures Result from Interactions Between R Groups
- Structure of the tertiary structure is determined by:
- Spatial distribution of hydrophilic & hydrophobic R groups.
- Different types of bonds (ionic, hydrogen, van der Waals) between R groups.
- Tertiary is made of several secondary structures.
- Tertiary shape is defined by the PRIMARY amino acid sequence.
Protein Denaturation
Protein unfolds because of chemical treatment, high temperature, pH change → hydrogen and ionic bonds are disrupted & protein loses functional activity.
Polysaccharide | Protein | Lipid | Nucleic Acid | |
Monomer | Monosaccharide E.g., glucose, carbohydrates | Amino acid NH3R-COOH | No true monomer | Nucleotide Ribose sugar |
Bond | Glycosidic | Peptide | Ester linkage | Phosphodiester |
Function | Structure/energy storage | Enzyme/transport/structure | Membrane/store energy | Information storage |
Unique | Highly branched | Functional 3D structure | No true monomer | 3′ & 2′ OH – RNA 3′ OH – DNA |
Direction | 4’C → 1’C | N → C | 5′ → 3′ |
Gibbs Free Energy
ΔG = ΔH + TΔS → entropy = motional freedom of a system & enthalpy = measure of how strongly bonded a system is.
Endosymbiosis Steps
- Aerobic bacteria were internalized by a protoeukaryotic host.
- Developed an endosymbiotic relationship.
- Transferred many bacterial genes into the host nucleus over time.
- Now semi-autonomous intracellular (mitochondrion).