Bio flashcards w/o unit 4
Deductive reasoning - big concept to specific situation (example: antibiotic resistance in bacteria to explain evolution/survival of the fittest)
Inductive reasoning - small concept to big concept (ex: beaks on birds to evolution)
Characteristics of living systems - made of cells, store and process information, transform energy, grow and reproduce, adapt and evolve
Cell theory - all organisms made of ells, cells smallest living things, cells arise from preexisting cells
Important chemical elements in living systems - CHON(P)
Cohesion - attraction between water molecules, allows for surface tension, form droplets
Adhesion - attraction between water molecules and other substances, drives capillary action
Function of enzymes - polymerases, proteases
Movement proteins - actin, myosin
Structural proteins- collagen, keratin
Defense proteins - antibodies, venoms
Nucleic Acids - building blocks for DNA, phosphodiester bond, 6-carbon sugar base, phosphate 5’, hydroxyl 3’
Proteins - made of AA, n-term (amino) c-terminus (carboxyl), peptide bond AA
Carbohydrates - made of monosaccharides, disaccharide bonds,
Polar - water lover, hydrophilic
Nonpolar - hydrophobic
Primary structure = amino acids
Secondary structure = flat sheet (b-sheet) or cylinder structure (a-helix), consist of hydrogen bonds
Tertiary structure = nonpolar buried in the middle of a protein, polar on surface of the structure
Quarternary structure = 2 or more polypeptide chains, between polypeptide chains
Nucleoid - prokaryotic, no membrane, DNA hanging out
Nucleus - eukaryotic w/ membrane, nucleus inside
Nucleolus - region inside nucleus, makes RNA structure for ribosomes
Prokaryotic - archaea and bacteria, unicellular and small and lack internal compartments; may have capsule, pili, flagella
Eukaryotic - animal and plant cells, has nucleus, ER and golgi apparatus, peroxisomes, and mitochondria; plants have chloroplasts and cell wall
Rough Endoplasmic Reticulum (ER) - network of membranes covered w/ ribosomes, involved in the synthesis and modification of proteins, transports proteins to other parts of the cell
Smooth Endoplasmic reticulum (ER) - network of membranes w/o ribosomes, involved in lipid synthesis, detox of harmful substances and stores Calcium ions
Golgi apparatus - modifies, sorts, packages proteins from the ER and transports them to destinations (in or out of the cell)
Lysosomes - aid in breakdown of old organelles, digestions of particles, trashcan
Peroxisomes - oxidation of fatty acids, biosynthetic reactions, detox
Vacuoles - store water, nutrients, water; in plants, central vacuole helps maintain cell structure; in animal cells, vacuoles are smaller and more specialized for storage/waste removal
Endosymbiosis - theory that forms mitochondria and chloroplasts; bacteria that performed oxidative metabolism (mito) or photosynthesis (chloro)
Cytoskeletal filaments - eukaryotic structure only, provide support, shape and organization to the cell
Actin - sliding mechanism for muscle contraction, microfilaments
Internal microtubules - cell organization and division,
External microtubules - cell swimming cilia and flagella
Intermediate filaments - keratin (skin) and lamins (surround nucleus of cells)
Cell membranes - composed of lipids and proteins, phospholipids provide structure of membrane and proteins provide functions; carbs sugar coat the surface of the membrane
How do membranes form? - polar hydrophilic head and 2 hydrophobic tails
Unsaturated - double bonds/kink in the chain
Saturated - no double bonds
Michelle - hydrophobic lipid tails cluster in the middle; heads from a h-bond with water
Bilayer - forms cell membranes, phospholipids held together by non-covalent interactions, selective permeability
Fluid mosaic model - 2D membrane where proteins are inserted or dissolved. extracellular on top and cytosolic face @ bottom
Integral membrane proteins - embedded in bilayer; transmembrane or lipid-anchored proteins
Peripheral membrane proteins - noncovalently bond to transmembrane proteins/phospholipid heads
Receptor proteins - allow cell to detect signal molecules and initiate cell’s response
Cell Identity - give ID, allows cell to be recognized by other cell
Enzymes - associate w/ different membranes, promotes chemical reactions to either face of membrane
Cell Adhesion - allow cell to attach to another cell or extracellular matrix
Cytoskeletal attachment - allows cell to transmit changes in cytoskeleton, changes in plasma membrane
Transport - movement of hydrophilic molecules from one side of membrane to other
Passive transport - no energy, molecules travel down gradients
Active transport - requires energy to travel up gradient
Coupled transport - movement of ion down gradient provides energy for another molecule to travel up its gradient
Symporters - ion and molecule transported in same direction across membrane
Antiporters - ion moves down its gradient, transports molecule in opposite direction
Osmosis - movement of water down its concentration
Hypertonic - pulls water out of cell, cell shrivels
Hypotonic - water floods cell, cell bursts
Endocytosis - allows eukaryotic cells to ingest larger martial from extracellular environment
Pinocytosis - cell drinking
Receptor-mediated - binds to specific receptor, triggers membrane to fold inward and form vesicle
Phagocytosis - cell eating
pH - go up pH, go lower in H+, factors of 10
Kinetic energy - energy of motion
Potential energy - stored energy
Oxidation - loss of electrons
Reduction - gain of electrons
1st Law of thermodynamics - energy cannot be created or destroyed
2nd Law of thermodynamics - entropy is continuously increasing
+delta G - products have more energy than reactants, not spontaneous, ENDERGONIC
-delta G - produced have less energy than reactants, spontaneous, EXERGONIC
Activation energy - energy required to initiate chemical reaction
How can you increase reaction rate? - heat molecules or use catalyst to lower activation energy
Catalysts - speed up reaction without being consumed or changed in the process, lower the activation energy, enzymes are biological catalysts
Inhibitor - molecule that binds to and decreases activity of an enzyme
Competitive inhibitor - competes w/ substrate for active site
Noncompetitive inhibitor - binds to enzyme at allosteric site that can cause shape changes that makes enzyme unable to bind to substrate
Biochemical pathways - reactions that occur in a sequence, product of one rxn is the substrate for the next rxn
feedback inhibition - end product of the pathway binds to an allosteric site on first enzyme in pathway
ATP - source of chemical energy, main energy for all cells
ATP & control of protein - provides energy for multiple processes such as activation or deactivation of proteins.
Phosphorylation - many proteins, like enzymes, are activated or inhibited through the addition or removal of phosphate groups; can change proteins shape, activity, stability or location
Autotrophs - makes own ATP and organic molecules via photosynthesis
Heterotrophs - lives on organic molecules produced by autotrophs
E-carriers - buckets that carry electrons and dump them elsewhere. (NAD+ to NADH)
Glycolysis - occurs in cytosol, generates 2 ATP molecules and 2 NADH molecules, breaks glucose into 2 pyruvate
Pyruvate Oxidation - occurs in mitrochondiral matrix, pyruvate into acetylCoA before entering krebs cycle, releases one CO2, reduced NAD+ to NADH
Krebs Cycle - occurs in matrix, forms citric acid with acetyl-CoA with oxaloacetate, 2 CO2 released, produces NADH, FADH2 and ATP
ETC - occurs in inner membrane, protein complexes in mitochondrial membrane, uses NADH and FADH2 electrons to power movement of H ions across the membrane to create a proton gradient, drives the synthesis of ATP, produces majority of the cell’s ATP
Chemiosmosis - process by which ATP is produced using the proton gradient of H+ ions across membrane. ETC pumps H+ into the intermembrane space and these protons flow back into the matrix through ATP synthase, central to oxidative phosphorylation
aerobic respiration - oxygen as final electron acceptor
Anaerobic respiration - inorganic molecules (like sulfur) as final electron acceptor, less ATP is produced
Fermentation - glycolysis is only source of ATP, organic molecule as final electron acceptor, reduces organic molecules to regenerate NAD+
Catabolize Proteins - proteins broken into AA, undergo deamination to remove amino group, remainder converted into a molecule that can enter glycolysis or krebs cycle
Catabolize fats - fats broken into fatty acids and glycerol, fatty acids are converted into acetyl group by B-oxidation, each acetyl group combines with CoA to make acetyl-CoA, enters krebs cycle
Photosynthesis - the inverse chemical formula of cellular respiration, energy for almost all life on earth comes from this process; occurs in chloroplasts
Light dependent reactions- require light, occur in thylakoid, capture energy from sunlight, make ATP and reduces NADP+ to NADPH, produces O2 as byproduct
Light Independent Reactions - doesn’t require light, occurs in stroma, use ATP and NADPH to synthesize organic molecules from CO2
Chlorophyll A - main pigment in plants, absorbs violet blue and red light, only pigment that converts light energy into chemical energy
Chlorophyll B - accessory pigment, absorbs blue and red-orange light, adds to range of absorbed light
Carotenoids - accessory pigment, absorbs blue and green light, adds to range of absorbed light, functions as an antioxidant
Photosystem II - absorbs light to excite electrons which are then passed into the ETC, splits water molecule to replace lost electrons to produce NADPH for calvin cycle
Photosystem I - absorbs light to re-energize electrons used to produce NADPH
How do light dependent reactions generate ATP and NADPH? - Absorption of light and electron excitation, ATP generation in photophosphorylation, protons flowing through ATP synthase to make ATP, NADPH produced by PSI which takes high energy electrons NADP+ with H+ to make NADPH.
Calvin Cycle - allows carbon fixation, RuBP + CO2 -> 2 PGA, PGA -> G3P, G3P used to regenerate Rubisco; 3 turns with the input of 3 CO2 to have enough carbon to produce new G3p; 6 turns to incorporate enough carbon for 1 glucose
Photorespiration - Carboxylation leads to carbon fixation and favored under normal conditions; oxidation leads to photorespiration and favored in dry conditions
C4 - use spatial solution, corn/sugarcane,
CAM - succulent plants, time-based, opens at night
Nucleotides consist of - adenine, thymine, cytosine, guanine, a phosphate group and a 5’ carbon sugar.
Where is a phosphodiester bond formed? - between phosphate and 3’ (OH) of another nucleotide
Watson and Crick DNA model - 2 nucleotide strande, complementary base pairs, constant diameter, strands are anti-parallel
DNA polymerase - enzyme that synthesizes DNA by adding nucleotides to a growing DNA strand during replication, works in 5’ to 3’ direction and requires template strand and primer to start synthesis, has a proofreading ability to ensure accuracy of DNA replication by correcting errors in base pairing
Continuous replication - synthesis of leading strand during DNA replication, same direction as the fork unwinds which means DNA polymerase can synthesize without interruption
Discontinuous replication - occurs on the lagging strand during DNA replication, so the lagging strand is synthesized in Okazaki fragments, these strands are later joined together by DNA ligase (glue) to form a continuous strand
Components required for DNA replication - DNA gyrase that relieves tension in strands, helicase unwinds the double helix, primase makes RNA primer, Polymerase III elongates, reads 3’ to 5’, synthesizes 5’ to 3’, DNA ligase is glue
Telomeres - DNA sequences at the end of chromosomes that protect them from damage (shoelace caps!) and prevent loss of important genetic info during replication.
Telomerase - enzyme that extends length of telomeres, extends the parental strand
Transcription - RNA synthesis, DNA to RNA
Translation - protein synthesis, RNA to protein/AA
Messenger RNA (mRNA) - codes for proteins
Robosomal (rRNA) - components of robosomes, catalyze protein synthesis
Transfer (tRNA) - adaptors between mRNA and AA
Small Nuclear (snRNA) - pre-mRNA splicing
MicroRNA (miRNA) - regulates gene expression
Initiation phase - subunit recognizes promoter, DNA unwinds ahead of start site, subunit released after ~10 subunits
Elongation phase - DNA synthesis 5’ to 3’
Termination phase - RNA base pairs w/ itself to create ‘hairpin’ formation, disrupts DNA/RNA/DNA pol interaction
Eukaryotic transcription - occurs in nucleus, 3 different RNA polymerase, termination phase not well defined, primary transcripts are processed to produce mature mRNA
Introns - non-coding regions that don’t need to be translated
Exons - coding regions that specify amino acids
Alternative splicing - single primary transcript may be spliced into different mRNAs by inclusion of different set of exons, can produce different proteins from a single gene
Critical features of genetic code - Initiation, elongation, termination, AA specified by sequence of 3 nucleotides (Codon),
Function molecules and phenotype - proteins are important to cell structure and function, and affect phenotype of an organism. A single nucleotide change in the gene that codes for hemoglobin changes the cellular phenotype from round to sickle-shaped.
Silent mutation - change to DNA nucleotide doesn’t alter AA
Missense mutation - change to DNA nucleotide changes AA
Nonsense mutilation - changes DNA nucleotide to a stop codon
Point mutilation - mutation that alters a single base
Frameshift mutilation - insertion of deletion mutation, changes downstream reading frame often with major consequences
Gene expression is controlled by 3 mechanisms - transcriptional regulation, post-transcriptional regulation, post-translational regulation
Positive control of transcription - activator protein is present, RNA polymerase can bind to binding site
Negative control of transcription - repressor protein is present, RNA polymerase cannot bind
Promoter region - DNA sequence upstream from transcription start site, RNA polymerase binds to the core promoter
Regulatory Proteins - affect ability of RNA polymerase to bind to the promoter/initiate transcription
Core promoter region - bound by sigma factor of RNA polymerase
Activator binding site - bound by positive control w/ activator proteins, can be closer to core promoter or further away
Operons - always have a promoter, but may have any number of activating binding sites and operators
Lac operon protein - produces proteins required for lactose metabolism
Lac repressor protein ___ transcription when lactose is ____ - inhibits, absent
CAP activator protein ___ transcription when glucose is ____ - promotes, absent
Induction - occurs when transcription from lac operon is stimulated by presence of lactose in the environment, environmental molecule stimulates transcription
Repression - occurs when tryptophan in the environment inhibits transcription from trp operon, molecule inhibits transcription
Chromatin - influence gene expression, DNA + histone organized into nucleosomes and then assembled in chromatin structure, changes in chromatin structure can occur by medical modification of histones or by ATP dependent movement of nucleosomes
Transcriptional regulation what is transcribed? - regulation by transcription factors, DNA accessibility
Post-transcriptional regulation what is translated? - regulation by mRNA processing, translation inhibition
Post-translational regulation how does protein function - regulation of protein stability, activity
Binary Fission - prokaryotic cells reproduce, replicate DNA and separate into 2 daughter cells
Mitosis - nonsexual cell division, end product diploid
Meiosis - sexual repo, end product haploid (sperm/eggs)
Haploid - complete set of chromosomes, necessary to define the species
Diploid - 2 complete set of chromosomes
Centromere - point at which chromatids stick together; kinetochore located
Kinetochore - ‘glue’ on centromere that stick to microtubules
Cohesion proteins - rubber bands holding sister chromatids together
Eukaryotic chromosomes - composed of chromatin, single chromosome is one continuous DNA molecule, there are 2 types of chromatin present in nucleus
Heterochromatin - tightly packed, inaccessibly, methylated histones,
Euchromatin - loosely packed, accessible, acetylated histones
M phase - nuclear division + cytoplasmic division
G1/S checkpoint - cell decides to divide, primary point for external signal influence
G2/S checkpoint - commitment to mitosis, double check DNA replication
Spindle checkpoint - cell ensures all chromosomes are attached to spindle, split before you check (nondisjunction)
G2 phase - centrosome duplicates, prep for M phase
Prophase - bipolar spindle assembles chromosomes conffense
Prometaphase - chromosomes attach to MTs, orient & congress
Metaphase - chromosome align at the spindle equator
Anaphase - sister chromatids separate, move to opposite poles
Telophase - chromosomes decondense nucleus begins to reform
Cytokinesis - cleavage furrow in animals, cell plate in plants
Deductive reasoning - big concept to specific situation (example: antibiotic resistance in bacteria to explain evolution/survival of the fittest)
Inductive reasoning - small concept to big concept (ex: beaks on birds to evolution)
Characteristics of living systems - made of cells, store and process information, transform energy, grow and reproduce, adapt and evolve
Cell theory - all organisms made of ells, cells smallest living things, cells arise from preexisting cells
Important chemical elements in living systems - CHON(P)
Cohesion - attraction between water molecules, allows for surface tension, form droplets
Adhesion - attraction between water molecules and other substances, drives capillary action
Function of enzymes - polymerases, proteases
Movement proteins - actin, myosin
Structural proteins- collagen, keratin
Defense proteins - antibodies, venoms
Nucleic Acids - building blocks for DNA, phosphodiester bond, 6-carbon sugar base, phosphate 5’, hydroxyl 3’
Proteins - made of AA, n-term (amino) c-terminus (carboxyl), peptide bond AA
Carbohydrates - made of monosaccharides, disaccharide bonds,
Polar - water lover, hydrophilic
Nonpolar - hydrophobic
Primary structure = amino acids
Secondary structure = flat sheet (b-sheet) or cylinder structure (a-helix), consist of hydrogen bonds
Tertiary structure = nonpolar buried in the middle of a protein, polar on surface of the structure
Quarternary structure = 2 or more polypeptide chains, between polypeptide chains
Nucleoid - prokaryotic, no membrane, DNA hanging out
Nucleus - eukaryotic w/ membrane, nucleus inside
Nucleolus - region inside nucleus, makes RNA structure for ribosomes
Prokaryotic - archaea and bacteria, unicellular and small and lack internal compartments; may have capsule, pili, flagella
Eukaryotic - animal and plant cells, has nucleus, ER and golgi apparatus, peroxisomes, and mitochondria; plants have chloroplasts and cell wall
Rough Endoplasmic Reticulum (ER) - network of membranes covered w/ ribosomes, involved in the synthesis and modification of proteins, transports proteins to other parts of the cell
Smooth Endoplasmic reticulum (ER) - network of membranes w/o ribosomes, involved in lipid synthesis, detox of harmful substances and stores Calcium ions
Golgi apparatus - modifies, sorts, packages proteins from the ER and transports them to destinations (in or out of the cell)
Lysosomes - aid in breakdown of old organelles, digestions of particles, trashcan
Peroxisomes - oxidation of fatty acids, biosynthetic reactions, detox
Vacuoles - store water, nutrients, water; in plants, central vacuole helps maintain cell structure; in animal cells, vacuoles are smaller and more specialized for storage/waste removal
Endosymbiosis - theory that forms mitochondria and chloroplasts; bacteria that performed oxidative metabolism (mito) or photosynthesis (chloro)
Cytoskeletal filaments - eukaryotic structure only, provide support, shape and organization to the cell
Actin - sliding mechanism for muscle contraction, microfilaments
Internal microtubules - cell organization and division,
External microtubules - cell swimming cilia and flagella
Intermediate filaments - keratin (skin) and lamins (surround nucleus of cells)
Cell membranes - composed of lipids and proteins, phospholipids provide structure of membrane and proteins provide functions; carbs sugar coat the surface of the membrane
How do membranes form? - polar hydrophilic head and 2 hydrophobic tails
Unsaturated - double bonds/kink in the chain
Saturated - no double bonds
Michelle - hydrophobic lipid tails cluster in the middle; heads from a h-bond with water
Bilayer - forms cell membranes, phospholipids held together by non-covalent interactions, selective permeability
Fluid mosaic model - 2D membrane where proteins are inserted or dissolved. extracellular on top and cytosolic face @ bottom
Integral membrane proteins - embedded in bilayer; transmembrane or lipid-anchored proteins
Peripheral membrane proteins - noncovalently bond to transmembrane proteins/phospholipid heads
Receptor proteins - allow cell to detect signal molecules and initiate cell’s response
Cell Identity - give ID, allows cell to be recognized by other cell
Enzymes - associate w/ different membranes, promotes chemical reactions to either face of membrane
Cell Adhesion - allow cell to attach to another cell or extracellular matrix
Cytoskeletal attachment - allows cell to transmit changes in cytoskeleton, changes in plasma membrane
Transport - movement of hydrophilic molecules from one side of membrane to other
Passive transport - no energy, molecules travel down gradients
Active transport - requires energy to travel up gradient
Coupled transport - movement of ion down gradient provides energy for another molecule to travel up its gradient
Symporters - ion and molecule transported in same direction across membrane
Antiporters - ion moves down its gradient, transports molecule in opposite direction
Osmosis - movement of water down its concentration
Hypertonic - pulls water out of cell, cell shrivels
Hypotonic - water floods cell, cell bursts
Endocytosis - allows eukaryotic cells to ingest larger martial from extracellular environment
Pinocytosis - cell drinking
Receptor-mediated - binds to specific receptor, triggers membrane to fold inward and form vesicle
Phagocytosis - cell eating
pH - go up pH, go lower in H+, factors of 10
Kinetic energy - energy of motion
Potential energy - stored energy
Oxidation - loss of electrons
Reduction - gain of electrons
1st Law of thermodynamics - energy cannot be created or destroyed
2nd Law of thermodynamics - entropy is continuously increasing
+delta G - products have more energy than reactants, not spontaneous, ENDERGONIC
-delta G - produced have less energy than reactants, spontaneous, EXERGONIC
Activation energy - energy required to initiate chemical reaction
How can you increase reaction rate? - heat molecules or use catalyst to lower activation energy
Catalysts - speed up reaction without being consumed or changed in the process, lower the activation energy, enzymes are biological catalysts
Inhibitor - molecule that binds to and decreases activity of an enzyme
Competitive inhibitor - competes w/ substrate for active site
Noncompetitive inhibitor - binds to enzyme at allosteric site that can cause shape changes that makes enzyme unable to bind to substrate
Biochemical pathways - reactions that occur in a sequence, product of one rxn is the substrate for the next rxn
feedback inhibition - end product of the pathway binds to an allosteric site on first enzyme in pathway
ATP - source of chemical energy, main energy for all cells
ATP & control of protein - provides energy for multiple processes such as activation or deactivation of proteins.
Phosphorylation - many proteins, like enzymes, are activated or inhibited through the addition or removal of phosphate groups; can change proteins shape, activity, stability or location
Autotrophs - makes own ATP and organic molecules via photosynthesis
Heterotrophs - lives on organic molecules produced by autotrophs
E-carriers - buckets that carry electrons and dump them elsewhere. (NAD+ to NADH)
Glycolysis - occurs in cytosol, generates 2 ATP molecules and 2 NADH molecules, breaks glucose into 2 pyruvate
Pyruvate Oxidation - occurs in mitrochondiral matrix, pyruvate into acetylCoA before entering krebs cycle, releases one CO2, reduced NAD+ to NADH
Krebs Cycle - occurs in matrix, forms citric acid with acetyl-CoA with oxaloacetate, 2 CO2 released, produces NADH, FADH2 and ATP
ETC - occurs in inner membrane, protein complexes in mitochondrial membrane, uses NADH and FADH2 electrons to power movement of H ions across the membrane to create a proton gradient, drives the synthesis of ATP, produces majority of the cell’s ATP
Chemiosmosis - process by which ATP is produced using the proton gradient of H+ ions across membrane. ETC pumps H+ into the intermembrane space and these protons flow back into the matrix through ATP synthase, central to oxidative phosphorylation
aerobic respiration - oxygen as final electron acceptor
Anaerobic respiration - inorganic molecules (like sulfur) as final electron acceptor, less ATP is produced
Fermentation - glycolysis is only source of ATP, organic molecule as final electron acceptor, reduces organic molecules to regenerate NAD+
Catabolize Proteins - proteins broken into AA, undergo deamination to remove amino group, remainder converted into a molecule that can enter glycolysis or krebs cycle
Catabolize fats - fats broken into fatty acids and glycerol, fatty acids are converted into acetyl group by B-oxidation, each acetyl group combines with CoA to make acetyl-CoA, enters krebs cycle
Photosynthesis - the inverse chemical formula of cellular respiration, energy for almost all life on earth comes from this process; occurs in chloroplasts
Light dependent reactions- require light, occur in thylakoid, capture energy from sunlight, make ATP and reduces NADP+ to NADPH, produces O2 as byproduct
Light Independent Reactions - doesn’t require light, occurs in stroma, use ATP and NADPH to synthesize organic molecules from CO2
Chlorophyll A - main pigment in plants, absorbs violet blue and red light, only pigment that converts light energy into chemical energy
Chlorophyll B - accessory pigment, absorbs blue and red-orange light, adds to range of absorbed light
Carotenoids - accessory pigment, absorbs blue and green light, adds to range of absorbed light, functions as an antioxidant
Photosystem II - absorbs light to excite electrons which are then passed into the ETC, splits water molecule to replace lost electrons to produce NADPH for calvin cycle
Photosystem I - absorbs light to re-energize electrons used to produce NADPH
How do light dependent reactions generate ATP and NADPH? - Absorption of light and electron excitation, ATP generation in photophosphorylation, protons flowing through ATP synthase to make ATP, NADPH produced by PSI which takes high energy electrons NADP+ with H+ to make NADPH.
Calvin Cycle - allows carbon fixation, RuBP + CO2 -> 2 PGA, PGA -> G3P, G3P used to regenerate Rubisco; 3 turns with the input of 3 CO2 to have enough carbon to produce new G3p; 6 turns to incorporate enough carbon for 1 glucose
Photorespiration - Carboxylation leads to carbon fixation and favored under normal conditions; oxidation leads to photorespiration and favored in dry conditions
C4 - use spatial solution, corn/sugarcane,
CAM - succulent plants, time-based, opens at night
Nucleotides consist of - adenine, thymine, cytosine, guanine, a phosphate group and a 5’ carbon sugar.
Where is a phosphodiester bond formed? - between phosphate and 3’ (OH) of another nucleotide
Watson and Crick DNA model - 2 nucleotide strande, complementary base pairs, constant diameter, strands are anti-parallel
DNA polymerase - enzyme that synthesizes DNA by adding nucleotides to a growing DNA strand during replication, works in 5’ to 3’ direction and requires template strand and primer to start synthesis, has a proofreading ability to ensure accuracy of DNA replication by correcting errors in base pairing
Continuous replication - synthesis of leading strand during DNA replication, same direction as the fork unwinds which means DNA polymerase can synthesize without interruption
Discontinuous replication - occurs on the lagging strand during DNA replication, so the lagging strand is synthesized in Okazaki fragments, these strands are later joined together by DNA ligase (glue) to form a continuous strand
Components required for DNA replication - DNA gyrase that relieves tension in strands, helicase unwinds the double helix, primase makes RNA primer, Polymerase III elongates, reads 3’ to 5’, synthesizes 5’ to 3’, DNA ligase is glue
Telomeres - DNA sequences at the end of chromosomes that protect them from damage (shoelace caps!) and prevent loss of important genetic info during replication.
Telomerase - enzyme that extends length of telomeres, extends the parental strand
Transcription - RNA synthesis, DNA to RNA
Translation - protein synthesis, RNA to protein/AA
Messenger RNA (mRNA) - codes for proteins
Robosomal (rRNA) - components of robosomes, catalyze protein synthesis
Transfer (tRNA) - adaptors between mRNA and AA
Small Nuclear (snRNA) - pre-mRNA splicing
MicroRNA (miRNA) - regulates gene expression
Initiation phase - subunit recognizes promoter, DNA unwinds ahead of start site, subunit released after ~10 subunits
Elongation phase - DNA synthesis 5’ to 3’
Termination phase - RNA base pairs w/ itself to create ‘hairpin’ formation, disrupts DNA/RNA/DNA pol interaction
Eukaryotic transcription - occurs in nucleus, 3 different RNA polymerase, termination phase not well defined, primary transcripts are processed to produce mature mRNA
Introns - non-coding regions that don’t need to be translated
Exons - coding regions that specify amino acids
Alternative splicing - single primary transcript may be spliced into different mRNAs by inclusion of different set of exons, can produce different proteins from a single gene
Critical features of genetic code - Initiation, elongation, termination, AA specified by sequence of 3 nucleotides (Codon),
Function molecules and phenotype - proteins are important to cell structure and function, and affect phenotype of an organism. A single nucleotide change in the gene that codes for hemoglobin changes the cellular phenotype from round to sickle-shaped.
Silent mutation - change to DNA nucleotide doesn’t alter AA
Missense mutation - change to DNA nucleotide changes AA
Nonsense mutilation - changes DNA nucleotide to a stop codon
Point mutilation - mutation that alters a single base
Frameshift mutilation - insertion of deletion mutation, changes downstream reading frame often with major consequences
Gene expression is controlled by 3 mechanisms - transcriptional regulation, post-transcriptional regulation, post-translational regulation
Positive control of transcription - activator protein is present, RNA polymerase can bind to binding site
Negative control of transcription - repressor protein is present, RNA polymerase cannot bind
Promoter region - DNA sequence upstream from transcription start site, RNA polymerase binds to the core promoter
Regulatory Proteins - affect ability of RNA polymerase to bind to the promoter/initiate transcription
Core promoter region - bound by sigma factor of RNA polymerase
Activator binding site - bound by positive control w/ activator proteins, can be closer to core promoter or further away
Operons - always have a promoter, but may have any number of activating binding sites and operators
Lac operon protein - produces proteins required for lactose metabolism
Lac repressor protein ___ transcription when lactose is ____ - inhibits, absent
CAP activator protein ___ transcription when glucose is ____ - promotes, absent
Induction - occurs when transcription from lac operon is stimulated by presence of lactose in the environment, environmental molecule stimulates transcription
Repression - occurs when tryptophan in the environment inhibits transcription from trp operon, molecule inhibits transcription
Chromatin - influence gene expression, DNA + histone organized into nucleosomes and then assembled in chromatin structure, changes in chromatin structure can occur by medical modification of histones or by ATP dependent movement of nucleosomes
Transcriptional regulation what is transcribed? - regulation by transcription factors, DNA accessibility
Post-transcriptional regulation what is translated? - regulation by mRNA processing, translation inhibition
Post-translational regulation how does protein function - regulation of protein stability, activity
Binary Fission - prokaryotic cells reproduce, replicate DNA and separate into 2 daughter cells
Mitosis - nonsexual cell division, end product diploid
Meiosis - sexual repo, end product haploid (sperm/eggs)
Haploid - complete set of chromosomes, necessary to define the species
Diploid - 2 complete set of chromosomes
Centromere - point at which chromatids stick together; kinetochore located
Kinetochore - ‘glue’ on centromere that stick to microtubules
Cohesion proteins - rubber bands holding sister chromatids together
Eukaryotic chromosomes - composed of chromatin, single chromosome is one continuous DNA molecule, there are 2 types of chromatin present in nucleus
Heterochromatin - tightly packed, inaccessibly, methylated histones,
Euchromatin - loosely packed, accessible, acetylated histones
M phase - nuclear division + cytoplasmic division
G1/S checkpoint - cell decides to divide, primary point for external signal influence
G2/S checkpoint - commitment to mitosis, double check DNA replication
Spindle checkpoint - cell ensures all chromosomes are attached to spindle, split before you check (nondisjunction)
G2 phase - centrosome duplicates, prep for M phase
Prophase - bipolar spindle assembles chromosomes conffense
Prometaphase - chromosomes attach to MTs, orient & congress
Metaphase - chromosome align at the spindle equator
Anaphase - sister chromatids separate, move to opposite poles
Telophase - chromosomes decondense nucleus begins to reform
Cytokinesis - cleavage furrow in animals, cell plate in plants