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Biology 107

"glossary"

TermDefinition
Water -universal solvent -polar -dipoles (allows for favorable interactions with other polar molecules) -high electronegativity
Covalent bonds -sharing of electrons in bonds -strong bond type
Ionic bonds -electron from one atom is fully associated with the other atom in the bond -strong bond type
Hydrogen bonds - dipole-dipole interactions (crucial in life) -weak bond type
Van der waals interactions -transient interaction of charges -very weak bond type
Organic molecules -contain H & C bonds -C is the backbone of organic molecules -C is weakly electronegative
Carbon -can bond to four other atoms -can form C-C chains -can form double and triple bonds with other C
Monomer -single building block of polymers
Polymer -form all macromolecules important to life
Dehydration synthesis (Condensation reaction) -adds monomers into polymer chains by catalyzing covalent bonds -water is a biproduct -requires energy
Hydrolysis -adds water to break a polymer chain -releases energy
Carbohydrates -Function: energy storage, cell structure, cell to cell recognition -Monomer (monosaccharides): have a C chain 3-7 C long, can be linear or ring shaped -Ex. Glucose (mono) and Sucrose (di) -glycosidic bonds
Polysaccharides - Starch (energy storage), glycogen (energy storage), cellulose (structure of cell wall), Chitin (structure)
Lipids (fats) - hydrophobic (nonpolar) -Fatty acids -> single chains of HC ending w/ COOH -16-18 C long -can attach to a 3C glycerol
Fats (triglycerides) -energy storage for animals -Can be saturated (straight tails) or unsaturated (kink in tails)
Phospholipids -Structural component of membranes -2 HC chains attached to a glycerol backbone via ester linkages with a phosphate group attached to the 3rd C of glycerol -amphipathic (both hydrophobic and philic ends)
Steroids (lipid-based cholesterol) -Function: Hormones (testosterone), major component of cell membrane in animals, modulate membrane fluidity, increases membrane stiffness
Proteins (polymer of a.a) -involved in every biological task -20 biological relevant a.a, (R-group) -directionality N-->C
*R-group 1)nonpolar -> R = HC 2)polar uncharged -> R group contains OH or SH 3) polar charged acidic -> R group contains COO- 4)polar charged basic ->R group contains NH2+
Structure of Proteins 1°-polymerization of a.a. (peptide bond) 2°- protein folding in alpha helix or beta pleated sheets 3°- 3D folding, hydrophobic R groups aggregate to the middle away from water which drives the folding 4°- globular units of multiple protein chains
Chaperones -proteins that assist in folding other proteins -proper folding is essential for proper function -if misfolded, they are degraded
Nucleic Acids (DNA/RNA) -Function: store and transmit hereditary info
DNA (molecule of heredity) - polymer of nucleotides - contains all info essential for life -transmits info between cell generations
RNA (transmits info with cell) -polymer of ribonucleotides -many functions: info transmission (mRNA), translation (tRNA & rRNA), regulation (siRNA & miRNA), splicing (snRNA)
Structure of ntd polymer -SC sugar=ribose, nitrogenous base, phosphate group -Pyrimidines-> cytosine, thymine, uracil (only RNA) -Purines -> guanine, adenine -Pyrimidine pairs with purine
Micelle -Conical -one tail -forms a circle with other phospholipids
Bilayer -Cylindrical -two tails
Phospholipid within bilayer -mobile (lateral movement common, flip flop rare) -flip flop movement facilitated by enzyme called flippine
Passive Transport -movement from high to low concentration -permeable substances only -osmosis
-tonic solutions -hypotonic-> water moves into cell (solute out), cell swells in mammals, doesn't in plants bc cell wall -isotonic-> no net movement of water -hypertonic->water moves out of cell (solute in), cell shrivels (plants = plasmolysis)
Facilitated diffusion - down concentration gradient -two types: channel & carrier proteins -impermeable substances need integral membrane protein to cross bilayer
Channel protein -integral membrane protein with a specific pore to allow passage of a solute
Carrier protein -integral membrane proteins that transport a solute using a conformational change -SPECIFIC -can be gated (open and close in response to stimulus) -highly regulated
Active Transport -Transport molecules up concentration gradient w/ energy -Used to: concentrate nutrients, expel waste, maintain electrochemical gradient -Ex. sodium/potassium pump -> maintains a charge difference across the membrane
Cotransport -transport of 2 molecules using the same transporter
Bulk transport - molecules too big to pass thru a transport protein must use a bulk transport mechanism -involves formation of vesicles -Exocytosis (out of cell), endocytosis (into cell), receptor mediated (carries specific molecules according to receptor)
Prokaryote -small -bacteria
Bacterial cell structure -DNA (circular genome), fimbrae (for attachment), cell wall & membrane, ribosomes, flagella (for movement) -NO membrane-bound organelles -BUT preforms all fxns eukaryotes can
Bacterial flagellum hook-> rotation about the hook allows movement filament- >composed of quaternary structure of flagellin -basil apparatus-> anchors filament to membrane = contains a gear system that allows rotation
Bacterial cell wall -Gram positive-> thick layer of peptidoglycan (PG), PG is a structural polysaccharide -Gram negative-> thin layer of PG surrounded by a lipopolysaccharide layer
Antibiotics -Function: kills bacteria pathogens by targeting bacterial specific structures-> bacterial cell wall and ribosomes
Microbiome -collection of micro-organization found in any given habitat
Eukaryotic cell structure -flagellum, microtubule organizing system, nucleus, nucleolus, rough & smooth ER, Golgi, mitochondria (mito),
Endomembrane system -Nucleus, nucleolus, nuclear envelope, ER, Golgi, lysosomes, vacuoles.
The nucleus -Function: most of the cell's DNA is stored in the nucleus arranged as linear chromosomes, chromatin packing (formation of chromosomes)
Nucleolus -Function: site for rRNA transcription and ribosomal subunit assembly
Nuclear envelope -Function: separates nucleoplasm from cytoplasm - double membrane bound -2 phospholipid bilayers (outer membrane is continuous to ER)
histone -positively charged protein used in chromatin packing -
Endoplasmic Reticulum (ER) -Rough ER: fxn-> site of protein translation & protein quality control. translation of proteins (called bound ribosomes) destined for the endomembrane system Smooth ER: fxn-> ion storage, phospholipid & steroid synthesis, detoxification of drugs/alchol
Golgi apparatus ("FedEx" of cell) -Structure: cisternae (flattened membrane bound faces), Cis, medial (modifies & sorts cargo), & trans faces -Golgi trafficking: vesicle trafficking (cargo moves thru from cis->medial->trans), cisternal maturation (MOST LIKELY, cis becomes medial etc)
Lysosomes (cell stomach) -digestion of macromolecules from phagocytosis -contains hydrolytic enzymes -pumps H+ into compartment -kept at low pH to avoid autophagy (self-eating)
Vacuoles -Fxn depends on cell type: food, contractile (pump out excess water), & central vacuole (specific to plants, storage & part of endomembrane system)
Plant cell wall -Fxn: maintains cell shape and prevents excess uptake of water and prevents osmotic lysis structure: main ingredient is cellulose
Stomata Openings that allow rapid exchange of nutrients and gases
Animal extracellular matrix (ECM) Fxn: maintains cell attachments across long distances, allows communication, maintains tissue integrity, stores growth factors Structure: secreted glycoproteins (collegen, fibronectin, integrin)
Collegen Forms the matrix of the ECM and connects cells over long distances
Fibronectin Links collegen to integrins
Integrins Proteins that link the ECM and MF
Epithelial cells -must stay connected to the ECM, if disconnected then commits cell suicide (apoptosis) Epithelial layers: layers of cells between you and environment (skin)
Cancer connection -90% of cancer occurs in the epithelium -epithelial cells are vulnerable to b/c exposed to carcinogens -major early step is loss of attachment to the ECM and failure to commit apoptosis
Animal cell-cell attachments -set of intercellular junctions in epithelial cells Fxn: maintain tissue integrity -three attachment types (Gap & tight junctions, desmosomes)
Tight junctions Fxn: act as rivets to seal cells together and prevent passage of molecules btwn cells and environment
Desmosomes Fxn: distribute stretching force across tissue and connect to adjacent cells exoskeleton via intermediate filaments
Gap junctions Fxn: provide non-selective transport of small molecules between adjacent cells and allows sharing and cell signaling (gap jxns in heart muscles allow for the spread of calcium btwn cells to signal contracting)
Metabolism -The totality of an organism's chemical rxns, managing the materials and energy resources of the cell -All of cells chemical rxns
Anabolism -Rxns that require energy to build the cell -linked w/ catabolism via ATP
Catabolism -Rxns that release energy from nutrient breakdown -linked w/ anabolism via ATP
Thermodynamics -The study of energy transformation/conversion
First law of Thermodynamics -Energy cannot be created nor destroyed
Second law of Thermodynamics -The energy of the universe is always increasing
Entropy -Measure of randomness/disorder of a system -heat is the most disordered form of energy -A rxn is spontaneous if the disorder of the universe increases out, then you can increase the order of the system
Free Energy -G (free energy) = H (total energy of a system) - T (temp) * ΔS (entropy) -High free energy = organized & low entropy -Low free energy = disordered & high entropy -Negative ΔG are spontaneous = exergonic --Positive ΔG are non-spontaneous = endergonic
Energy coupling -Energy from exergonic rxns are used to power endergonic rxns -can be direct coupling by coupled transport w/ the release of Na+ -Can be indirect w/ ATP
ATP (Adenosine Triphosphate) -The cellular energy currency -Bonds that join the three phosphates onto adenosine are high energy bonds and store energy -Hydrolysis of these bonds release energy = exergonic (ΔG = -13 kcal/mol) -Contains PE due to position and composition
Enzymes (-ase) -Biological catalysts that provide an alternate energy path for a rxn to proceed -Rxn in both endergonic and exergonic rxns -HIGHLY regulated
Autotroph "self-feeders" -Use inorganic CO2 as C source, fix to organic C (highly endergonic) -Photoautrophs = use light energy to power fixation -Chemoautotrophs = use redox rxn energy to power C fixation (only bacteria)
Heterotroph -Use organic C as C & energy source -Chemoheterotrophs = use organic C as main nutrients -Photoheterotrophs = use light energy & organic C (bacteria)
Chloroplast -Site of photosynthesis -double membrane bound with stacks of internal membrane called thylakoids -Stroma = site of the calvin cycle -Thylakoid lumen = site of light rxns
Photosynthesis (6 CO2 + 6 H2O + light -> C6H12O6 + O2) -O2 is waste -CO2 is reduced to glucose
Light reactions Use energy carried by light & convert it into chemical energy in the form of ATP & NADPH which are used to drive the calvin cycle
Light absorbed -Absorbed by pigments -absorbed energy is usually released as heat or fluorescence (unless energy is converted) -Photosystems capture light energy & convert it to chemical energy
The Photosytems -contain pigments such as chlorophyll (main), xanthophylls, carotenoids, etc. -absorbed light excites e- and moves them through the photosystems
Electron transport chain (ETC) photosynthesis -A set of increasing strength e- acceptors -allows energy from excited e- to be converted into a H+ chain releasing energy
Energy conservation of Photosynthesis Photosystems (1) = convert light energy into chemical energy in the form of an excited e- ETC (2&3) = 2) excited e- passes through an ETC & releases energy via redox rxns used to pump H+ and create a gradient. 3) excited e- from P(i) used to reduce NADP+
Chemiosmosis -Formation of ATP using H+ gradient & ATP synthase -Respiration = oxidative phosphorylation Photosynthesis = photophosphorylation
ATP synthase An enzyme complex that couples an endergonic rxn (ADP + P(i)-> ATP) with an exergonic process (dissipation of H+ gradient)
Calvin cycle POINT: to fix C by the conversion of atmospheric to organic (highly endergonic) -three phases: Carbon fixation, Reduction, and Regeneration
Carbon fixation One CO2 molecule per turn of cycle. Turn cycle 3 times to produce one G3P w/ the enzyme Rubisco
Reduction The NADPH from light reactions is used to reduce fixed C (NADPH donates e-)
Regeneration RuBp inhibits Rubisco to regulate carbon fixation
Cyclic Electron flow -If ATP is low in chloroplast, excited e- goes back to ETC to be pumped through and create ATP w/o NADPH
Respiration -Catabolic (energy releasing) -POINT: Complete oxidation of glucose & convert to energy -Three phases: Glycolysis, Krebs cycle, ETC -Occurs in mito -pyruvate "decides" to enter the mito to complete respiration (controlled by the availability of O2)
Glycolysis -The conversion of glucose to pyruvate -POINT: to begin the oxidation of glucose
Transition reaction -oxidation of pyruvic acid to Acetyl CoA when pyruvate enters the mitochondria -catalyzed by pyruvate dehydrogenase (PDH)
Krebs cycle (TCA/Citric Acid cycle) -POINT: complete oxidation of glucose -O2 released, occurs in matrix of mitochondria, 2 ATP produced by SLP
ETC (respiration) -Across the MIM -e- from NADH or FADH2 are used in redox rxns to power H+ pumping. FADH2 donates e- at a lower energy level (complex II)
Fermentation -POINT: recycle NAD+ for continued glycolysis in eukaryotes -Pyruvate is reduced to waste & acts as an e- acceptor -2 pathways: Lactic acid and Ethanolic
Ethanolic Fermentation -when oxygen is NOT available, some cells have the capacity to undergo fermentation
Cell division (mitosis) Key roles: Reproduction: unicellular organisms divide to produce offspring Development: Multicellular eukaryotes are composed of many cells which arose by mitosis of a single fertilized egg
Prokaryote cell division (binary fission) -Simpler than mitosis (only one chromosome) -creates 2 genetically identical daughter cells
Prokaryotic growth curve 1) Lag phase: cells growing but not dividing 2) Log phase: all cells are dividing 3) Stationary phase: cell death, nutrients and space become limiting 4) Death phase: death>division due to accumulation of wastes and depletion of nutrients
Eukaryotic cell division -Multiple linear chromosomes inside a nucleus -creates 2 genetically identical daughter cells
Chromosome -one copy of genetic info, chromatid product of DNA replication. -Chromatids attach in a chromosome at a centromere -Kinetochore = protein complex that assemble at the centromere
Cell cycle 4 distinct phases: -G1: normal cell activities, cell is "deciding" to divide -S: Synthesis phase (DNA replication) -G2: normal cell activities, cell preparing to divide (2x DNA) -M: Mitosis, separation of chromatids
Mitosis -unique cell cycle phase where the DNA is equally separated into daughter cells -6 phases: prophase, prometaphase, metaphase, anaphase, telophase, cytokinesis
Prophase -MAIN PROCESS: Chromosomal condensation, packaging of chromosomes into fully condensed mitotic chromosomes -cell with 2 chromosomes -Microtubules (MT) are responsible for moving chromosomes around cell
Prometaphase -MAIN PROCESS: nuclear envelope break down (NEBD), MT polymerization invades nuclear area to attach to kinetochore or centromere -MT grow and shrink until they contact a kinetochore (fishing)
Metaphase -MAIN PROCESS: line up chromosomes at metaphase plate/division plane -Chromosomes are moved by pol/depol of MT (primary force)
Anaphase -MAIN PROCESS: separation of sister chromatids (each molecule of DNA is now called a chromosome) -Kinetochore MT pull chromosomes to pole by depol dynein
Telophase -MAIN PROCESS: nuclear envelope reformation, chromosomal decondensation.
Cytokinesis -MAIN PROCESS: separation of cytoplasm -Actin filaments bundle a cytokinetic ring and myosin constricts it -eventually the contractile ring separates cytoplasm into 2 daughter cells
Cell cycle control 3 checkpoints -> decision points to decide when a cell should divide -Restriction (G1) checkpoint, G2 check point, Metaphase checkpoint. If cell passes the requirements cell division continues
Cancer -uncontrolled cell division, ~90% of all cancers are epithelial in origin -cancers are accumulations of random mutations that cause uncontrolled cell division -ignore restriction checkpoints
DNA -carries genetic information -double helix -complementary base pairing (A-T, C-G) -antiparallel (5'-3', 3'-5') -purine pairs with pyrimidine
Griffiths Transformation experiment -Asked "is there a transforming principle?" -proved the existence of a transforming principle (an abiotic factor that carries hereditary info)
Avery, Macleod and McCarty experiment -Asked "what is the transforming principle?" -concluded that DNA was the transforming principle
Hershey and Chase (phage-in-a-blender) experiment -Asked "is DNA the universal transforming principle?" -used radioactive material to detect if the DNA or protein entered the bacteria -concluded that DNA is the universal transforming principle
Chemical composition of DNA -sugar-phosphate backbone -phosphodiester bonds -H bonds between bases (provides specificity) -Base stacking = hydrophobic <- main stabilizing force of double helix
DNA replication -Semi-conservative replication: products of replication are composed of one daughter strand and one parent strand -Daughter strands are complementary copies of parent template
Meselson-Stahl experiment -wanted to determine which hypothetical process of DNA replication was correct (conservative, semi-conservative, or dispersive) -concluded that semi-conservative replication was the correct model
Helicase unwinds parental double helix at replication fork
Single-strand binding protein Binds to and stabilizes single-stranded DNA until it can be used as a template
Primase Synthesizes an RNA primer at 5' end of leading strand and of each Okazaki fragment of lagging strand
DNA pol III Using parental DNA as a template, synthesizes new DNA strand by covalently adding ntds to the 3' end of a pre-existing DNA strand or RNA primer
DNA pol I Removes RNA ntds of primer from 5' end and replaces them with DNA ntds
DNA ligase Joins the 3' end of DNA that replaces primer to rest of leading strand and joins Okazaki fragments of lagging strand
Flow of information DNA (store info) --transcription(trxn)--> mRNA (info transmission) --translation--> protein (info use)
Gene (general) -Stretches of DNA that contain hereditary info (unit of heredity) -all genes must have a promoter (site of RNA pol assembly) -Promoter = sequence of DNA that transcription factors bind to -multiple genes in chromosome
Transcription -occurs 5' to 3' (DNA read 3' to 5') - uses template strand, coding strand not used -Transcript = RNA product -enzyme of transcription is RNA polymerase
Prokaryotic gene -Conserved elements that direct gene expression (TATA box) -TATA box = rich AT sequence found before transcription starts -Transcription factors (TFs): proteins that can read DNA at TATA box (recruits RNA polymerase)
Eukaryotic gene -Lots of different DNA elements that regulate transcription (combinatorial control) -has enhancer elements (DNA) that activator protein binds to -initiation complex involves multi-subunit looping of DNA to enhance RNA polymerase binding
Translation The process in which genetic code carried by mRNA directs the synthesis of proteins to amino acids
Exons amino acid encoding regions which contain expressed sequences found in both a gene's DNA and mature mRNA (coding)
Introns non-amino acid encoding regions which contain intervening sequences found in a gene's DNA but not in the mature mRNA (non-coding)
tRNA adapter molecules that mediate the transfer of information from nucleic acids to proteins antiparallel & complementary base pairs w/ codon in mRNA. can recognize more than one codon for the a a they carry. two regions: a a folding & mRNA binding region
Aminoacyl tRNA synthetase (the translator) -Correct matching of tRNA and its associated a. a. -20 different synthetases for the 20 different a. a. -fxn: pairs the a. a. to tRNA based on anticodon sequences
Ribosomes -catalyze peptide bonds -Facilitate the specific coupling of tRNA codons during protein synth -Two major subunits: large ribosomal subunit, small ribosomal subunit and its assoc rRNA -large contains 3 sites: A= approach p= Polymerization & E = exit
Created by: ldquinn
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