Chapter 1: Themes in the Study of Life
1.1 Biology
Emergent properties: properties that are not present at the preceding level
o Complexity increases: tissue→ cell→ organ→ organ system
Reductionism: reducing complex systems o simpler components for study
Systems biology: approach that attempts to model the dynamic behavior of whole biological systems based on the study of the
interactions of the system’s parts
o Predict how change in one variable affects other components
Ecosystem Organization
1. Biosphere: all life on earth and where life exists
2. Ecosystem: forest, grassland, desert,; all living/nonliving things in a particular area
3. Communities: entire array of organisms in a particular area; trees, plants, fungi
4. Populations: all individuals of a species within a specific area
5. Organisms: individual living things
6. Organs and organ systems: stems, roots, brain, heart
7. Tissues: skin (epidermis)
8. Cells: single and multi-celled organisms; specialized cells (muscle, nerve)
9. Organelles: various functional components present in cells; chloroplasts
10. Molecules: chemical structure consisting of 2+ atoms; chlorophyll
Eukaryotic: multi-celled organism
Prokaryotic: lack membrane enclosure and nucleus
DNA (deoxyribonucleic acid): stored in chromosomes; is the substance of genes
Enzymes: catalysts for specific chemical reactions
Gene expression: info in a gene that directs production of a cellular product
o Differences b/w organisms are changes in nucleotide sequence, not genetic code
RNA: translated into proteins; some manufactures protein
Genome: entire “library” of genetic instructions that is inherited
Negative feedback: accumulation of and end process slows that process
Positive feedback: end product speeds up own production
Cell’s breakdown of sugar produces ATP
1.2 Evolution
1. Species: ursus americanus
2. Genus: ursus
3. Family: ursidae
4. Order: carnivore
5. Class: mammalia
6. Phylum: chordata
7. Kingdom: animalia
8. Domain:
a. Bacteria: rod-shaped
b. Archaea: round and live in extreme environments
c. Eukarya: plantae, fungi, protists, animalia
Natural selection: Charles Darwin
1. Individuals in a population vary in traits which seems to be heritable
2. Populations produce more offspring than can survive; competition
3. Species generally suit their environments; adaptation
1.3 Observations and Hypothesis
Inductive reasoning: collecting and analyzing observations to lead to important conclusions
Deductive reasoning: used after hypothesis developed
o General to specific
Theory: encompass multiple hypotheses
Scientific fact: well-tested and confirmed but may be rejected in the future
Discovery science: descriptive or observational science
1.4 Cooperative Approach and Diverse Viewpoints
Model organism: a species that is easy to grow in a lab and lends itself particularly well to questioning Chapter 2: The Chemical Context of Life
2.1 Elements and Compounds
Essential elements: 20-25% of 92 elements needed to support life
o 25 for humans, 17 for plants
Oxygen, carbon, hydrogen, nitrogen make up 96% of living matter
o Phosphorus, potassium, and sulfur account for remaining 4%
Trace elements: required by an organism in minute quantities
2.2 Element Properties Depend on the Structure of Atoms
Dalton: unit of measure for atoms and subatomic particles; amu
Atomic number of protons (bottom number)
Mass number: sum of protons and neutrons (top number)
Isotope: same number of protons but different number of protons
o Radioactive isotope: ones in which the nucleus decays spontaneously
Energy: capacity to cause change
Potential energy: energy matter possesses based on location or structure
2.3 Formation and Function of Molecules
Valence: bonding capacity
Substrates: reactants
Ionic compounds: salts
Biological molecules: can bond temporarily if shapes are complementary
o Opiates, pain relievers
2.4 Making and Breaking Chemical Bonds
Chemical equilibrium: point at which reactants offset one another because of stabilized ratios
o Reaction still occurs but with no net change in concentrations
Chapter 3: Water and Life
3.1 Polar Covalent Bonds in H O2Result in Hydrogen Bonding
Each hydrogen in H O has partial positive charge b/c oxygen more electronegative
2
3.2 Four Emergent Properties of H O2Contribute to Earth’s Suitability for Life
Cohesion: linking together of like molecules often by H-bonding
o Allows transport of H2O and dissolved nutrients against gravity
Adhesion: clinging of one substance to another
o Adhesion of H 2 to cell walls by H-bonding counters gravity
Heat: measure of the total KE die to the motion of particles
o Heat depends on volume
Temperature: measure of heat intensity
o Average KE regardless of volume
Calorie: amount of heat required to raise the temp. of 1g 2f H O by 1°C
Joule: 1joule=0.239cal / 1cal=4.184J
Heat of vaporization: quantity of heat a liquid must absorb for 1g of liquid to turn into gas
Evaporative cooling: hottest molecules with most KE leave as a gas
o As liquid evaporates, the surface of the liquid cools
Crystalline structure is less dense so ice floats b/c of empty space and molecules move too slowly to break H-bonds
Hydration shell: sphere of 2 O molecules around each dissolved ion
Colloid: stable suspension of fine particles in a liquid
o Mostly large molecules like cellulose (partial charges can form H-bonds but not dissolve)
3.3 Acidic and Basic Conditions Affect Living Organisms
pH=-log[H ]
+
Buffer: substance that accepts H from solution when in excess and donates when depleted
o weak acid and conjugate base
Ocean acidification: CO2dissolves in seawater to react wit2 H O to form carbonic acid which lowers pH
Acid precipitation: pH lower than 5.2 Chapter 4: Carbon and the Molecular Diversity of Life
4.1 Organic Chemistry if the Study of Carbon Compounds
Major elements of life: C, H, O, N, S, and P
4.2 Carbon Atoms can Form Diverse Molecules by Bonding to Four Other Atoms
CO d2batable as organic since it lacks hydrogen
Hydrocarbons: organic molecules consisting of only hydrogen and carbon
o Undissolvable in H 2 b/c hydrophobic and relatively nonpolar
o Can undergo reactions that produce relatively large amounts of energy
Isomers: variation in the architecture of organic molecules
1. Structural: differ in covalent arrangements
a. Saturated: fully bonded carbon chain with hydrogens
i. > energy with more bonds
b. Unsaturated: double bonds present
2. Geometric: arrangement around double bond
3. Optical/mirror/enantiomers: asymmetric carbon
4.3 Few Chemical Groups are Key to the Functioning of Biological Molecules
1. Hydroxyl: alcohols
a. Polar b/c oxygen so can form H-bonds that dissolve organic molecules
2. Carbonyl: keytones(within) & aldehydes(end)
a. Found in sugars
3. Carboxyl: carboxylic acids/organic acids +
a. Acts as an acid b/c can donate H to ionize
4. Amino: amines
a. Acts as a base b/c can pick up H from solutions
5. Sulfhydryl: thiols
a. 2 sulfhydryl groups form a covalent bond: cross-liking stabilizes protein structures
6. Phosphate: organic phosphates (ATP)
a. Potential to react with 2 O
7. Methyl: methylated crystals
a. Nonpolar
Chapter 5: Structure and Function of Large Biological Molecules
5.1 Macromolecules are Polymers, Built from Monomers
Polymer: long molecule consisting of many similar or identical building blocks linked by covalent bonds
Macromolecules: carbohydrates, proteins, and nucleic acids
5.2 Carbohydrates Serve as Fuel and Building Materials
Carbohydrates: include sugars and polymers of sugars
Monosaccharides: generally have formula that is multiple of CH O 2
o Glucose is most common
o Used for cellular respiration and synthesis of amino and fatty acids
Glycosidic linkage: joins a disaccharide with a covalent bond through dehydration
o Sucrose
Polysaccharides: polymers with 100s to 1000s of monosaccharides
1. Storage: starch is a polymer of sucrose monomers; glycogen stored in animal liver and muscle cells and hydrolysis of these
releases glucose
a. Amylose: unbranched
b. Amylopectin: branched with 1-6 linkages
2. Structural: build polysaccharides
a. Cellulose: major component in tough walls that enclose plant cells
b. Chitin: carbohydrate used by arthropods to build exoskeletons 5.3 Lipids are a Diverse Group of Hydrophobic Molecules
Lipids: hydrophobic and are not large enough to be considered macromolecules
1. Fats: glycerol and fatty acids; purpose is to store energy
o Glycerol: alcohol that has 3 carbons each with hydroxyl group
Triacylglycerol: 3 fatty acid molecules with glycerol linked by esther
Esther: bond b/w hydroxyl and carboxyl
o Fatty acids: 16-18 carbons with carboxyl at one end
Saturated: only single bonds with as many H as possible; unhealthy
Unsaturated: one or more double bonds and has kinks so cannot pack as closely
Cis double bond: causes bonding and prevents solidifying at room temp.
Trans fat: formed artificially during hydrogenation of oils
2. Phospholipids: make up cell membranes
3. Steroids: carbon skeleton with 4 fused rings
o Cholesterol: animal cell membranes, synthesis of hormones
Viscosity buffer system in phospholipid bilayer
5.4 Proteins Include Diversity of Structures therefore Wide Range of Functions
Polypeptides: polymers of amino acids
o Protein: molecule of 1 or more polypeptides
Amino acid: amino and carboxyl group
o Side chain determines each amino acid
Acidic aminos have (-) side charge and vice versa
Peptide bond: carboxyl group with amino bond formed through dehydration
Globular or fibrous proteins
Function depends on its ability to recognize and bind to other molecules
Levels of Protein Structure:
1. Primary: linked series of amino acids with unique sequence
2. Secondary: alpha helix coils and beta pleated sheet folds (cellulose) that contribute to overall shape
a. Interaction between backbone
b. Result of H-bonds
3. Tertiary: overall shape of polypeptide from interactions between side chains
a. Hydrophobic interaction: as poly folds into shape, nonpolar side chains cluster in middle (hydrophobic)
b. Van der Waals hold together nonpolar; H-bonds for polar
c. Disulfide bridges: 2 cysteine monomers with sulfhydryl groups brought together
4. Quaternary: overall protein structure from aggregation of polypeptide subunits
Sickle-cell disease: inherited blood disorder b/c substitution of one amino acid for another (valine for glutamic acid) at a particular
position in hemoglobin
o Abnormal hemoglobin molecules crystalize and deform cells to sickle shape
Denaturation: weak bonds and interactions cause protein to unravel and lose its shape
Chaperonins: crucial to folding process and keeps “bad influences” out
o Alzheimer’s and Parkinson’s from accumulation of misfolded proteins
X-ray crystallography: used to determine the 3D structure of proteins
Nuclear magnetic resonance (NMR): spectroscopy that does not require protein crystallization
5.5 Nucleic Acids Store, Transmit, and Help Express Hereditary Info
Gene: discrete unit of inheritance
Nucleic acid: polymers made of nucleotides
o Polynucleotides: DNA & RNA
Pyrimidine: cytosine, uracil, thymine
6-membered ring of carbon and nitrogen
Purine: adenine, guanine
6-membered ring fused with 5-member ring
Double helix: 2 polynucleotides
Antiparallel: 2 sugar phosphate backbone run opposite directions 5’→3’
DNA: provide instructions for its own replication, directs RNA synthesis, and controls protein synthesis in ribosomes
o RNA: conveys genetic instruction for building proteins from nucleus to cytoplasm
Transfer RNA (tRNA): brings amino acids to the ribosome during polypeptide synthesis
nd
o Deoxyribose and ribose: deoxyribose lacks an oxygen on 2 carbon in ring Chapter 6: A Tour of the Cell
6.1 Microscopes and the Tools of Biochemistry
Organelles: membrane-enclosed structures in eukaryotic cells
Cell fractionation: takes cells apart and separates major organelles through centrifuge
Electron microscope: focuses a beam of electrons through specimen or onto surface
o Resolution varies inversely to wavelength of radiation
Scanning electron microscope: detailed study of topography of a specimen
Transmission electron microscope: internal cell structure viewable by staining with heavy metals to enhance electron density
6.2 Eukaryotic Cells Compartmentalize Their Functions
Cytosol: jellylike substance in which subcellular components are suspended
Nucleoid: region of prokaryotic cells where DNA is not membrane-bound
Microvilli: long, thin projections that increase surface area w/o much increase in volume
6.3 Eukaryotic Genetic Instructions in Nucleus and Carried Out by Ribosomes
Nucleus enclosed by nuclear envelope
o Double membrane with pore complex that regulates entry/exit of proteins
Nuclear lamina: netlike array of protein filaments that hold nucleus shape
o Chromatin: complex of DNA and proteins that make up chromosomes
Nucleolus: ribosomal RNA synthesized from imported proteins
Ribosomes: made of rRNA and proteins
1. Free: suspended in cytosol; make proteins for function in cytosol
2. Bound: attached to outside
6.4 Endomembrane System Regulates Protein Traffic and Performs Metabolic Functions
Endoplasmic reticulum: network of membranes
o Important for ER to make new components b/c ER shrinks every time vesicles departs
o ER lumen/cisterna space: internal compartment of the ER
o Glycoproteins: proteins that have carbohydrates
1. Rough: studded with ribosomes; protein synthesis
2. Smooth: outer surface lacks ribosomes, metabolic processes and enzymes; storage of ions, detox, fats production
Golgi apparatus: warehouse for receiving, sorting, and
o Cis face: receiving; vesicles can add their contents to cis face by fusing with Golgi
o Trans face: shipping; vesicles that pinch off and travel to other sites
Lysosome: membranous sac of hydrolytic enzymes used to digest (hydrolyze) macromolecules; acidic
Phagocytosis: intercellular digestion of smaller organisms of food particles
o Autophagy: use of hydrolytic enzymes to recycle cell’s own organic material
Vacuole: large vesicles derived from ER and Golgi
o Food: formed by phagocytosis
o Contractile: pump excess H O out of cell to maintain concentration
2
o Central: coalescence of smaller vacuoles that contains inorganic ions; only in plant cells
6.5 Mitochondria and Chloroplasts Change Forms of Energy
Mitochondria: sites of cellular respiration; uses oxygen to generate ATP by extracting energy from sugars and fats
o Mitochondrial matrix: enclosed by the inner membrane and contains mitochondrial DNA and ribosomes; respiration
proteins
Chloroplasts: 2 phospholipid bilayers and composed of thylakoid
o Thylakoids: flattened, interconnected sacs; stacked like poker chips
Granum: each stack of thylakoids
Stroma: fluid outside thylakoids
Cristae: foldings in the inner membrane
Plastids: one of a family of closely related organelles that include chloroplasts
o Amyloplast: colorless organelle that stores starch
o Chromoplast: orange and yellow pigments
Peroxisomes: metabolic compartment bounded by single membrane
o H2O 2s toxic so enzyme converts H2O2to H 2 2
o Glyoxysomes: fat-storing tissues of plant seeds
Fatty acid to sugar for energy until self-sufficient with photosynthesis 6.6 Cytoskeleton is a Network of Fibers that Organizes Structures and Activities
Cytoskeleton: network of fibers through cytoplasm
o Microtubules: hollow rods of alpha and beta tubulin
Dimer: molecule made of 2 subunits
Centrosome: microtubule organizing center
Centrioles: 1 pair per centrosome
Flagella and cilia: microtubule-containing extensions
Basal body: anchors microtubule assembly
Dyneins: large motor protein that connects doublets
o Microfilaments: solid rods of twisted double chain of actin to hold shape
Cortex: outer cytoplasmic layer supported by network
Myosin: motor protein by means of projections that walk on actin filaments
Pseudopodia: “false foot”; extension by actin subunits
o Intermediate filaments: named for diameter; bears tension and fixes organelle positions
6.7 Extracellular b/w Cells Help Coordinate Cellular Activities
Middle lamella: thin layer of pectins that glues adjacent cells together
Plasmodesmata: perforated channels b/w cytoplasm of adjacent cells
Extracellular matrix (ECM): glycoprotein and other carbohydrates
o Collagen most abundant glycoprotein
Proteoglycan molecules: core protein with carbs attached
Proteoglycan complexes: PG molecules join with long polysaccharides
o Fibronectin: bind to cell-surface receptors called integrins
Integrins: cell surface receptor proteins
Gap junction: connects cytoplasm and communicates with intermediate filaments
Tight junction: bands that circle all the way around and limit leakage
Desmosome: adhere with plaques of proteins
Chapter 7: Membrane Structure and Function
7.1 Cellular Membranes are Fluid Mosaics of Lipids and Proteins
Integral proteins: penetrate hydrophobic interior of bilayer
Peripheral proteins: appendages bound loosely to membrane surface
Protein Functions:
1. Transport: selectively permeable hydrophilic channel; may change shape to accommodate
2. Enzymatic activity: protein built into membrane may be an enzyme
3. Signal transduction: membrane protein receptor has shape that fits a specific chemical message
4. Cell-cell recognition: glycoproteins serve as i.d. tags that are specifically recognized by membrane proteins
5. Intercellular joining: membrane proteins of adjacent cells hook together in gap or tight junctions
6. Attachment to cytoskeleton and ECM: microfilaments or other elements noncovalently bind to membrane proteins to maintain
cell shape and stabilize location
Glycolipids: covalent bond of carb and lipid
o Glycoprotein: covalent bond of protein and lipid
7.2 Membrane Structure Results in Selective Permeability
Transport proteins: allow hydrophilic or polar ions t pass through membrane
o Channel proteins: have hydrophilic channel for molecules
o Carrier proteins: hold passengers and change shape to pass membrane
7.3 Passive Transport is Diffusion of a Substance w/o Energy Investment
Concentration gradient: represents PE and density
Tonicity: ability of a surrounding solution to cause a cell to gain/2lose H O
o Isotonic, hypertonic, hypotonic
o Plants are happiest in hypotonic environment
Osmoregulation: control of the concentration of the solute’s an2 H O balance
o Turgor pressure: back pressure on cell that opposes further H O uptake
2
Turgid and flaccid
Plasmolysis: as plant cell shrivels, plasma membrane pulls away from the cell wall
7.4 Active Transport Uses Energy to Move Solutes against Gradients
Sodium-potassium pump: exchanges Na for K across plasma membrane to induce protein to change shape that translocates a solute
bound to protein across the membrane
Membrane potential: voltage from -50 to -200m with cytoplasmic side: (-) so favors cations in
o Drives diffusion
Electrogenic pump: generates voltage across membrane
o Proton pump: plant version; H out of cell; uniport: one direction
o Cotransport: single port that transports specific solute and indirectly drives active transport of other solutes 7.5 Bulk Transport across Plasma Membrane by Exocytosis and Endocytosis
1. Phagocytosis: cell engulfs a particle by wrapping pseudopodia
2. Pinocytosis: cell engulfs droplets
3. Receptor-mediated: enables cell to acquire in specific bulk
Ligands: low-density lipoproteins: molecules that bind specifically to a receptor site on another molecule
Chapter 8: An Intro Into Metabolism
8.1 An Organism’s Metabolism Transforms Matter & Energy Subject to the Law of Thermodynamics
Metabolism: totality of an organism’s chemical reactions
o Cell at metabolic equilibrium is dead
o Metabolic pathway: specific and organized; allows for amplification
Catabolic: release energy by breaking don molecules
Cellular respiration: glucose broken down with O to form CO + H O
2 2 2
Anabolic: consumes energy to build complicated molecules
Photosynthesis
Synthesis of amino acids and then synthesis of proteins from amino acids
Energy: capacity to cause change; ability to rearrange a collection of matter
o Thermal energy: KE associated with random movements of atoms and molecules
Thermodynamics: study of energy transformations
o Isolated systems: unable to exchange energy or mater with its surroundings
o Open system: able to exchange
1. First Law: energy transferred, not created nor destroyed
2. Second
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