I. Cell

Key focus of this chapter: biological macromolecules

This chapter focuses on biological macromolecules and gives concise summaries of the important things about cell membrane and cellular respiration in more detail.

A. Biological Macromolecules

Most biological molecules are composed primarily of carbon (C), hydrogen (H), oxygen (O), nitrogen (N), phosphorus (P), and sulfur (S), collectively known as CHNOPS.

  • Nucleic acids: C, H, O, N, and P
  • Proteins: primarily C, H, O, and N; some proteins also contain S

1. Carbohydrates (Sugars)

  • Composed primarily of carbon, hydrogen, and oxygen, often in an approximate 1:2:1 ratio
  • Functions: energy source, energy storage, structural support, and cell recognition

Carbohydrates (sugar)

Classification

Description

Monosaccharide

Glucose

• A six-carbon aldose sugar; the primary energy source for most cells

Ribose

• A five-carbon sugar found in RNA

Deoxyribose

• A five-carbon sugar found in DNA

Galactose

• A component of lactose

Fructose

• A six-carbon ketose sugar found in many fruits; a component of sucrose

Disaccharide

Sucrose

• Glucose + fructose

• α(1→2)β glycosidic linkage

Maltose

• Glucose + glucose

• α(1→4) glycosidic linkage

Lactose

• Glucose + galactose

• β(1→4) glycosidic linkage

Polysaccharide

Starch

• A glucose-storage polysaccharide in plants

• Composed of amylose and amylopectin

• Contains α(1→4) linkages and α(1→6) branch points

Glycogen

• A highly branched glucose-storage polysaccharide in animals and fungi

• Contains α(1→4) linkages and α(1→6) branch points

• More highly branched than starch

Cellulose

• The primary structural polysaccharide of plant cell walls

• Composed of β-glucose monomers joined by β(1→4) glycosidic linkages

• Parallel cellulose chains are linked by hydrogen bonds to form microfibrils

Chitin

• A structural polysaccharide composed of N-acetylglucosamine (NAG) monomers

• A major component of fungal cell walls and arthropod exoskeletons

2. Proteins

a. Amino acid

  • Subunit of proteins as a monomer.
  • Consisting of amino group, carboxyl group, a carbon, functional group, and hydrogen.
  • Each of 20 common amino acids has different functional group.

 b. Polypeptide

  • Amino acids are linked by peptide bonds.
  • Multiple functions such as enzyme catalysis, hormone, storage, regulation, defense, transport, support, and motion.
  • Heating or changing condition of pH causes protein to lose its secondary, tertiary, or quaternary structure and becomes inactive.

Structures

Features

Primary (1º) structure

• Unique linear amino acid sequence; peptide bonds.

Secondary (2º) structure

• α-helices and β-pleated sheets; stabilized by hydrogen bonds between backbone atoms.

Tertiary (3º) structure

• Overall 3D shape of a single polypeptide; stabilized by hydrogen bonds, ionic interactions, disulfide bonds, van der Waals forces, and hydrophobic interactions among R groups.

Quaternary (4º) structure

• Association of two or more polypeptide subunits into one functional protein; Example: hemoglobin.

3. Lipid

a. Fat

  • Unsaturated fat presences of double bond, which causes kink in fatty acid tail, increases fluidity.

– eg/oil

  • Saturated fat presences of no double bond, which causes no kink, decreases fluidity.

– eg/butter

  • Greatest source of energy producing 9 calories/gram.

** Carbohydrate and protein produce 4 calories/gram.

– eg/ glycerol, fatty acid, triacylglycerol

b. Phospholipid

  • Forming amphipathic (hydrophilic and hydrophobic) bilayers of cell membrane.

c. Steroids

  • Four fused carbon rings.
  • Keep fluids inside the membrane.
  • Found in most animal cell membranes.
  • eg/cholesterol

4. Nucleic acids

  • Molecules that store genetic information of organisms.
  • Composed of nucleotide (five carbon sugar, nitrogenous base, and phosphate group).
  • Phosphate groups connected by phosphodiester bonds.
  • Two nucleic acids connected by hydrogen bonds.
  • Anti-paralleled strands.

Classification

Description

Nucleoside

Five-carbon sugar + nitrogenous base

Nucleotide

Five-carbon sugar + nitrogenous base + phosphate group

Nucleic acids

Polymer of nucleotides linked by phosphodiester bonds

DNA structure of biological macromolecules

DNA

RNA

Sugar

Deoxyribose

Ribose

Bases

A, G, C, T

A, G, C, U

Structure

Usually double-stranded

Usually single-stranded

Bonds

Hydrogen bonds (between strands) and phosphodiester bonds

Phosphodiester bonds

B. Shapes and functions of the cells

1. Cell theory

  • The smallest unit of life functions
  • Basic units of all living organisms
  • All cells coming from other cells

2. The difference between prokaryotic and eukaryotic cells

Prokaryotic cell

Eukaryotic cell

• Cell division by binary fission

• Can exchange genetic material by conjugation

• Nucleoid (lacks a nuclear envelope)

• Mitotic and meiotic division

• Generally larger than prokaryotic cells

• Nucleus (w/ nuclear envelope)

• Organelles with membrane

3. Structure of prokaryotic and eukaryotic cells

Structures

Prokaryote

Eukaryote

Plant

Animal

Cell wall

Existence

(peptidoglycan)

Existence

(cellulose)

None

Cytoplasm

Existence

Existence

Existence

Ribosome

Existence

Existence

Existence

Cytoskeleton

Existence

Existence

Existence

Nucleoid

Existence

None

None

Nucleus

None

Existence

Existence

Mitochondria

None

Existence

Existence

ER, Golgi

None

Existence

Existence

Chloroplast

None

Existence

None

Vacuole

None

Existence

(major)

Existence

(minor)

Centriole

None

None

Existence

Lysosome

None

None

Existence

a. The functions of organelles

Organelles

Functions and features

Flagella

• Cell locomotion

Nucleus

• DNA replication and transcription

• Stores genetic information

Ribosomes

• Site of protein synthesis.

• Ribosomal subunits are assembled in the nucleolus.

• Functional ribosomes are found in the cytoplasm, mitochondria, and chloroplasts.

• Free in the cytoplasm or bound to the rough endoplasmic reticulum (ER).

• Composed of rRNA and proteins.

Rough ER

• Studded with ribosomes.

• Synthesizes secretory proteins, membrane proteins, and membrane components.

Smooth ER

• Lacks ribosomes

• Lipid synthesis (including steroid hormones)

• Calcium storage

• Carbohydrate metabolism

• Detoxification

Golgi Apparatus

• Receives proteins and lipids from the ER.

• Modifies, sorts, and packages proteins and lipids.

• Ships vesicles from the trans face to the plasma membrane or other destinations.

Lysosomes

• Membrane-bound organelles containing hydrolytic enzymes.

• Formed through the Golgi apparatus.

• Primarily found in animal cells.

Peroxisomes

• Contains oxidative enzymes that produce and break down H₂O₂.

• Oxidizes fatty acids and detoxifies harmful compounds.

• Formed from the ER.

Vacuole

• Stores nutrients and waste products.

• Isolates harmful substances.

• Maintains internal pH and turgor pressure.

• Surrounded by the tonoplast membrane.

Mitochondria

• Site of aerobic cellular respiration and ATP production.

• Contains its own ribosomes and DNA.

• Double membrane, cristae, and matrix.

• Originated through endosymbiosis.

Chloroplasts

• Site of photosynthesis.

• Contains its own ribosomes and DNA.

• Double membrane, stroma, thylakoids, and chlorophyll.

• Originated through endosymbiosis.

Cytosol

• Main site of many metabolic reactions, including glycolysis.

Centriole

• Organizes microtubules

• Helps form the mitotic spindle during cell division

• Found primarily in animal cells

b. Cytoskeletons

Cytoskeletons

Functions and features

Microtubules

• Hollow tubes composed of tubulin

• Form the mitotic spindle during cell division

• The axoneme of cilia and flagella has a 9+2 microtubule arrangement

• Major component of centrosomes and centrioles

• Form cilia and flagella (with dynein for movement)

• Serve as tracks for intracellular transport by kinesin and dynein

Microfilaments
(Actin filament)

• Cleavage furrow in cytokinesis

• Cell crawling (amoeboid movement)

• Support the cell cortex and microvilli

• Interact with myosin during muscle contraction

Intermediate filaments

• Tensile strength

• Nuclear lamina

• Keratin provides mechanical strength to epithelial cells.

c. Different layers of membranes

Membranes

Organelles

No membrane

Centriole, Ribosome

Single membrane

Peroxisome, Lysosome, ER, Golgi apparatus, Vacuole

Double membrane

Chloroplast, Mitochondria, Nucleus

d. Extracellular matrix

• Collagen is the most abundant structural protein in animals and forms a triple-helix structure.

e. Endomembrane system

** Simplified pathway for DAT review. Some lipids may follow alternative intracellular transport pathways.

f. Growth of cell

  • Surface area increases by 10².
  • Volume increases by 10³.

C. Cell communication

Cells communicate with one another to coordinate growth, development, and responses to environmental signals.

1. Signal

a. Direct cell-to-cell communication

Cell types

Classification

Features

Animal cell

Tight junction

Tightly associated membranes between two cells

Gap junction

Channels that directly connect the cytoplasm of adjacent cells

Desmosomes

Anchoring junctions held together by adhesion proteins

Plant cell

Plasmodesmata

Perforated channels in plant cell wall

b. Local signal

  • Paracrine signal

– Signaling molecules diffuse through the extracellular fluid to nearby target cells.

– Local distance

– Eg/ Growth factors, clotting factors, histamines, nitric oxide

  • Synaptic signal

– Release of neurotransmitters into the synaptic cleft.

c. Long distance signal

  • Endocrine signal

– Hormones are released into the bloodstream and travel to distant target cells.

– Long distance

– Eg/ Estradiol, testosterone, adrenaline, insulin

2. Reception

a. Cell surface reception

 Receptor that binds signal on plasma membrane.

  • Ion channel linked receptors

– Acting as gate controlling synaptic signaling by. neurotransmitter.

  • G-protein linked receptors

– Activate G proteins, which relay signals to intracellular effector proteins and enzymes.

  • Receptor Tyrosine kinases

– Ligand binding activates receptor tyrosine kinases, which use ATP to phosphorylate themselves and intracellular proteins.

b. Intracellular reception

Intracellular receptors bind hydrophobic signaling molecules, such as steroid hormones, inside the cell.

3. Transduction

a. Phosphorylation cascade

A series of protein kinase activations in which each kinase phosphorylates and activates the next kinase.  

  • Phosphorylation

– Protein kinase: An enzyme that transfers phosphate groups from ATP to target proteins.

– Protein phosphatase: An enzyme that removes phosphate groups from proteins.

b. G protein signaling pathway

  • A first messenger binds to and activates a G protein-coupled receptor.
  • Adenylyl cyclase converts ATP to cAMP.
  • cAMP acts as a second messenger and activates protein kinase A (PKA).

c. Calcium and IP₃ signaling pathway

  • A first messenger binds to and activates a G protein-coupled receptor.
  • Phospholipase C (PLC) hydrolyzes PIP₂ into two second messengers: IP₃ and DAG.
  • IP₃ binds to IP₃-gated Ca²⁺ channels in the endoplasmic reticulum, causing Ca²⁺ to be released into the cytosol.

  • Ca²⁺ acts as a second messenger and activates various target proteins.
  • DAG, together with Ca²⁺, activates protein kinase C (PKC).

4. Response

The cellular response may involve changes in gene expression or cytoplasmic activity.

D. Membrane

1. Function

  • Separates the inside of the cell from the outside environment.
  • Selectively transports molecules into and out of the cell.
  • Allows cell growth and movement.
  • Enables communication with other cells.

 2. Components of structure

  • Phospholipids – Form a bilayer; each phospholipid has a hydrophilic head and hydrophobic tails.
  • Proteins – Integral (transmembrane) proteins and peripheral proteins.
  • Cholesterols – Embedded in the membrane and helps maintain membrane fluidity under different environmental conditions.
  • Glycolipids – Function in cell recognition and cell-to-cell communication.
  • Fluid Mosaic Model – The membrane is a dynamic structure composed of phospholipids, proteins, and cholesterol.

 3. Passive transport

Movement of substances from a region of higher concentration to a region of lower concentration.

  • Does not require energy.
  • Simple diffusion occurs directly through the phospholipid bilayer.
  • Facilitated diffusion requires transport proteins but does not require ATP.

  • Water moves by osmosis through aquaporins.

a. Diffusion

  • Net movement of molecules from an area of higher concentration to an area of lower concentration due to random molecular motion.
  • Eg/ Movement of O2 and CO2 across cell membrane, movement of dissolved solutes in a solution.

 b. Osmosis

  • Diffusion of water across a selectively permeable membrane from an area of high water potential to an area of low water potential.
  • Eg/ Water moves through aquaporin channels in cell membranes.
  • If cell is placed in

– Hypotonic solution: Animal cells àLysed, Plant cells à Turgid

* Because of absorption of water, the cell size becomes bigger.

* Eg/ A red blood cell swells up and bursts when it is placed in distilled water.

– isotonic solution: Animal cells → Normal, Plant cells → Flaccid

– hypertonic solution: Animal cells → Shrunken (crenated), Plant cells → Plasmolyzed

* Because of losing water, the cell size shrinks.

4. Active transport

: movement of substances from an area of low concentration to an area of high concentration by using chemical energy.

  • Requires energy.
  • Eg/ Sodium-potassium pump of axon, electrogenic pump, cotransport (symport and antiport), proton pump.

5. Bulk transport

: movement of large molecules across the membrane.

Classification

Features

Endocytosis

Pinocytosis

Engulfing liquid by using vesicle of membrane

Phagocytosis

Engulfing particles by using of membrane

Receptor-mediated

endocytosis

Engulfing molecules by specific receptor of vesicle membrane

Exocytosis

Ejection of stuff in vesicle by plasma membrane

E. Energy and life

1. Metabolism

: energy property from the chemical reaction to maintain living organisms

  • Catabolic pathways – breakdown pathway or digestive process.
  • Anabolic pathways – the process of building complicated molecules from smaller units by using energy.

2. Laws of energy

a. First law of thermodynamics

  • Principle of conservation of energy – energy can be transferred and transformed, but not created or destroyed.
  • Eg/Chemical energy converts into kinetic energy after eating food.

b. Second law of thermodynamics

  • Universal law of increasing entropy.
  • Eg/ Heat energy emit when organisms work.

3. Homeostasis

: control system to maintain the stable internal condition from outside environmental changes.

  • Negative feedback.

– reversal change of internal condition against outside environmental changes.

– most homeostatic animal cells operate on negative feedback.

  • Positive feedback – same directional change of internal condition with outside environmental change.

F. Enzymes

: a biological catalyst (mainly protein) increasing the chemical reaction by lowering the activation energy without being used up.

  • Enzymatic conformational change by binding substrate.
  • No changing concentration of product, Keq, ΔS, or ΔG by enzyme.
  • Influenced enzyme by temperature, pH level, concentration of enzyme, and concentration of substrate.
  • Each enzyme having certain optimum temperature and pH.
  • Reusable enzyme after finishing catalytic activity.

1. Reaction

  • Exergonic reaction: release of free energy.
  • Endergonic reaction: obtaining free energy.

 2. Structure of enzyme

  • Allosteric site

– meaning different site.

– regulatory molecules (activator, inhibitor) binding site.

  • Active site – substrate binding site

3. Regulation of enzyme

a. Allosteric Enzyme

: enzyme can be active or inactive by the binding of regulatory molecule to allosteric site.

  • Activation – products are produced by binding of activator at allosteric site.
  • Inhibition – products are not produced by binding of inhibitor at allosteric site.
  • Cooperativity.

– binding one substrate to active site causes the rest of the subunits to be stimulated and become active.

– amplify the activity of enzyme.

 b. Enzyme with inhibition

  • Non-competitive inhibition

– binding inhibitor to the allosteric site causes the enzyme to be inactive.

  • Competitive inhibition

– binding inhibitor to the active site hinders the binding activator to active site and becomes inactive.

  • Feedback inhibition

– the end product of a long series of enzymatic reaction inhibits the beginning reaction of the series.

G. Photosynthesis

1. Redox reaction

a. Oxidation

  • Losing electron and hydrogen.
  • Gaining oxygen.

b. Reduction

  • Gaining electron and hydrogen.
  • Losing oxygen.

** OILRIG – Oxidation Is Losing electron and Reduction Is Gaining electron.

 2. Chloroplast

: double membraned organelle of cell, which is to convert light energy to chemical energy.

a. Structure of chloroplast

b. Larger to smaller structure

c. Photosynthesis

: converting light energy to ATP free energy and reducing NADP to NADPH to make sugar as a final product.

  • Light + 6H2O + 6CO2 →  C6H12O6 + 6O2
  • Occurring in some bacteria, algae, and plants.

i. Light dependent (light reaction)

  • Taking place at thylakoid membrane.
  • Photosynthetic pigments (light receptors).

: magnesium-containing porphyrin ring and hydrocarbon tail in Chlorophyll.

– chlorophyll a: primary pigment with reflection of blue-green light.

– chlorophyll b: accessory pigment with reflection green-yellow light.

– carotenoid: accessory pigment with reflection of yellow-red light and photoprotection (protection of chlorophyll by dissipating excessive light energy).

  • H2O is source of electron, hydrogen, and oxygen at photosystem II.

   H2O (split into)    →   e, H+, O2           

  • Final product of photosystem II (P680) is ATP from electron transport system.
  • Final product of photosystem I (P700) is NADPH from electron transport system.
  • The movement of H+ across a membrane through cytochrome complex is active transport.
  • The movement of H+ across a membrane through ATP synthase is facilitated diffusion.

ii. Light independent (dark reaction)

  • Takes place in stroma.
  • Uses ATP and NADPH to produce sugar in Calvin cycle.
  • Calvin cycle

RuBP (Ribulose bisphosphate) + CO2 (by Rubisco enzyme)

  →    Two 3-phosphoglycerate (PGA) per turn of Calvin cycle

  • Glyceraldehyde 3-phosphate (PGAL): immediate food nutrient, glucose formation, and end product of Calvin cycle

d. Photosynthesis in C3, C4, CAM plants

  • C3 plants

– Eg/ Most crops (rice, wheat, soybeans).

  • C4 plants

– adaptation in hot and dry conditions.

– spatial separation: CO2 fixation in mesophyll cell and then working of Calvin cycle in bundle sheath cell.

– eg/ sugarcane, corn.

  • CAM plants

– adaptation in arid conditions.

– temporal separation (night, day) – CO2 enter into stomata during night and then working of Calvin cycle during day.

– open stomata during the night and close stomata during the day.

– eg/ Cacti, pineapples.

H. Cellular respiration

: metabolic reaction, which is to convert nutrients into energy in organism cells

  • Glycolysis, fermentation, mitochondria (TCA cycle, electron transport chain)

 C6H12O6 + 6O  6H2O + 6CO2 + Energy (ATP)

1. Glycolysis

: metabolic pathway, which is to convert one glucose into two pyruvates in cytosol.

  • Investing 2ATP and harvesting 4ATP, therefore harvesting net 2ATP.
  • Harvesting 2NADH, 2H+, 2H2O, 2Pyruvates.

Glucose + 2NAD+ + 2Pi + 2ADP   →   2Pyruvates + 2NADH + 2ATP(NET) + 2H+ + 2H2O

2. Fermentation

: ATP production in anaerobic respiration.

  • Glucose → pyruvate → lactate (lactic acid), ethanol.
  • Lactate reaction in muscle cell.
  • Ethanol reaction in yeast cell.
  • Lactic acid goes the cori cycle in the liver to regenerate glucose again.
  • Regeneration of NAD+

3. Mitochondria

: double membraned organelle of cell, which is place for oxidative metabolism to make ATP.

  • Aerobic respiration

a. Structure of mitochondria

  • Double membrane
  • Cristae
  • Matrix
  • Krebs cycle

b. Acetyl CoA

  • Aerobic metabolism in mitochondria before moving into Krebs cycle
  • Production of 2CO2, 2NADH, and 2H+

c. Krebs cycle (Citric acid cycle, TCA cycle)

  • Aerobic metabolism in mitochondria
  • Acetyl CoA + oxaloacetate acid → citrate
  • Producing 6 NADH, 2 FADH2, 2 ATP (2 GTP), and 4 CO2 per 2 pyruvates (1 glucose molecule = 2 pyruvates)

d. Catabolism of various macromolecules

  • Gluconeogenesis – glucose generation of metabolic pathway from amino acid, glycerol, and lactate.

 e. Electron transport

  • Electron transport chain and chemiosmosis at inner mitochondrial membrane are called oxidative phosphorylation.
  • Ubiquinone and cytochrome c are mobile lipid-soluble carriers of electron.
  • Electron transport chain pumps protons from matrix to intermembrane space to increase a proton gradient.
  • The created proton gradient synthesizes ATP.
  • Production 32 or 34 ATP (1NADH=3ATP, 1FADH2=2ATP).
  • O2 is final source for acceptance of electron from NADH and FADH2 to become H2O.

4. Overall reaction between photosynthesis and cellular metabolism

a. Chloroplasts

  • PS II and electron transport: O2 and 18 ATP/6 turns (1 glucose = 6 turns)
  • PS I and electron transport: 12NADPH/6 turns
  • Calvin cycle: 12 PGAL/ 6 turns, glucose

b. Mitochondria

  • Krebs cycle: 4 CO2, 6 NADH, 2ATP, and 2 FADH2/ per 2 pyruvates
  • Electron transport chain: 32 – 34 ATP, H2O

c. ATP producing in cellular respiration per 1mole glucose: 36 – 38 ATP

  • Glycolysis: 2 ATP
  • Krebs cycle: 2 ATP
  • Electron transport chain: 32~34 ATP

d. Mitochondria and chloroplasts

  • Semiautonomous containing DNA and ribosome
  • Endosymbiosis