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Principles of Bio 1

Fist Midterm

QuestionAnswer
Biology Defined scientific study of living organisms
"materialism" reality is based off of matter, energy, and information (the known physical forces)
"vitalism" opposite of materialism. forces of energy based on unobserved information
where do mass, energy, and information come from? mass and energy come from enviornment. and information is inherited from your parents
what defines "life"? life arises via reproduction and evolution of previously existing life
metabolic aspect of life life is a process with continuous input and output of matter and energy (atoms are not permanent residents)
hierarchy of biological organization ecosystem -> organism -> organs -> tissues -> cells -> organelles -> molecules -> atoms . . .
essential elements of life 25 out of 92 total elements are required major elements - H,C,O,N (96% of total by mass)
importance of shape of molecules responsible for recognition and response in biology (enzyme specificity, membrane transport, signal recognition)
polymer formed by covalently linking monomers ex.) starch, proteins(polypeptides), and DNA RNA
benefits of polymers you can make many different polymers with a small number of monomers -> allows for coping with changing needs
hydrolysis reaction breaks bonds between monomers of a polymer through the use of water (spontaneous reaction)
dehydration reaction removes water molecule forming a covalent bond between to monomers (non-spontaneous) DOES NOT OCCUR IN CELLS!!!
synthesis of polymers activated monomer loses OH molecule and covalently bonds to polymer transfer from activated monomer is spontaneous and does occur in cells
proteins polymers of amino acids - catalytic, structural, transport, and receptor proteins (different structure, different functions)
components of an amino acid amino group (H-N-H) R group (side chain) Carboxyl group (O-C-OH)
primary structure of a protein linear sequence of amino acids
secondary structure of a protein 2 structures 1.) beta pleated sheet structure 2.) alpha helix
tertiary structure of a protein side chains interact to form complex folds to compact structure
quarternary structure of a protein includes all tertiary secondary and primary structures
denaturation protein is unraveled in a sense
renaturation protein reverts back to its normal structure (not always possible)
catalytic cycle of an enzyme substrates fit into specific active site in enzyme and are changed into the products
enzyme inhibition competitive inhibitor binds to active site not allowing substrate to be catalyzed
allosteric inhibitor non-competitive inhibition, inhibitor binds to opposite side of enzyme
prokaryotes no nucleus or membrane enclosed organelles ex.) bacteria, archaea
eukaryotes has nucleus and membrane enclosed organelles ex.) multicellular organisms
cytoplasm cytosol, organelles, and cytoskeleton
cell fractionation separating the parts of a cell to study individually
pellet and supernatant pellet is at the bottom of the test tube during cell fractionation and the supernatant is the rest
nucleus double membrane with nuclear pores and nuclear lamina chromatin DNA ->RNA nucleolus rRNA
ribosomes 2 subunits (large and small) assembled in nucleolus - membrane bound and free - made of proteins and RNA - site of protein synthesis
chromatin made of DNA and protein -DNA -> RNA in nucleolus
endoplasmic reticulum rough and smooth - membrane network of tubes, flattened sacs inside the cytoplasm
rough ER -protein synthesis (membrane, secretory, and other) -carbohydrate attachment to form glycoproteins -phospholipid synthesis (membranes)
smooth ER -tubes connected without ribosomes -synthesis of lipids -detoxification (drugs and alcohol)
nuclear lamina in nucleus -exoskeletal fibers under membrane
golgi apparatus -carbohydrates on glycoproteins get modified -secretory polysaccarides -cells "postal service"
lysosomes bags of digestive enzymes -active at low pH's (~5) -autophagy (self eating) cells "sewage treatment plant"
phagocytosis lysosome digesting food (protist)
autophagy breaking down damaged organelle
cytoskeleton -microtubules -microfilaments -intermediate filaments Functions : maintain cell shape, allows changes in cell shape, supports movement w/in cell, anchors organelles, cell motility site (amoeba, cilia, flagela)
cell membrane basic structure is similar, dynamic Functions : barrier (selectively permeable), sensor, and adhesion (to form tissues)
phospholipids amphipathic -> both hydrophilic and hydrophobic -major molecule of membranes -formed from triglycerides (glycerol + fatty acids) -self assembled -> bilayer (b/c of hydrophilic and hydrophobic ends)
integral proteins proteins inside of the membrane (through the middle of the membrane)
peripheral proteins proteins outside of the membrane
G-Protein coupled receptor (GPCR) -receives signal from molecule outside -G-Protein inside binds to receptor and changes GDP to GTP
membrane fluidity depends on lipid composition and temperature - tails with kinks are fluid - saturated tails w/out kinks are viscous
carbohydrates in membranes found on the outsides of cell membrane -glycoproteins -glycolipids -oligosaccharides
functions of membrane proteins -transport -enzymatic activity -signal transduction -intercellular joining -cell-cell recognition -attachment to the cytoskeleton and extracellular matrix
tight junctions -seal, separate adjacent cells -prevent fluid and solutes from moving across a layer of cells
desmosomes anchor cells to one another
gap junctions intercellular communications
membrane permeability fat soluable and non-polar molecules permeate ex.) hydrocarbons, CO2 and O2 Polar and ionic molecules need special path by means of channels and transporters
passive movement high to low concentration (diffusion free or mediated)
active movement low to high concentration
facilitated diffusion -Channels -Molecules move passively –high to low concentration -Channels and Carriers show substrate specificity -Carriers (Transporters) -passive transport
cystic fibrosis chloride channel defect
channels Specific pathways - Allow diffusion - Some are open in default position - Some are closed in default position - Can be closed or opened by specific conditions
active transport low -> high concentration - requires input of energy
membrane potential electrical force -inside is typically more negative than the outside
electrogenic pumps - Proton (H+) pump - generates Proton Gradient - each proton carries 1 positive charge - generates Membrane Electrical Potential (Voltage)
sodium potassium pump -requires ATP -phosphate becomes covalently bonded to protein - 3 Na+ out and 2 K+ in results in overall negative 1 charge
electrochemical gradient - Membrane potential (electrical force) - Concentration difference (chemical force) - Energy gradient (osmotic force)
essential properties of genes - Contain information - Can be replicated precisely (almost) - Can produce observable traits
evidence supporting DNA as genetic material viruses grow in bacteria -DNA entered cell and proteins didn't so DNA was source of making genes
chemical components of DNA - Deoxyribose - Nitrogenous bases - Phosphate
deoxyribose 5 carbon sugar
pyrimidines Cytosine and Thymine - single ring
Purines Adenine and Guanine - double ring
hydrogen bonds in base pairing A-T --> 2 hydrogen bonds C-G --> 3 hydrogen bonds
semiconservative model each "daughter" DNA has 1 parent strand and 1 new strand
conservative model after replication there is 1 parent molecule and 1 entirely new DNA molecule
dispersive model 2 new strands are both a mixture of parent and new strands
Meselson-Stahl Experiment solidified that the semiconservative model is the correct model for replication
origin of replication starts in bubbles along strand until whole strand is separated ===<>====<>===<>===
synthesis of new DNA - One nucleotide added at a time - Precursor = deoxynucleosidetriphosphate, which provides energy as well as mass - only goes from 5' to 3' direction
topoisomerase relieves the unwinding strain
Helicase unwinds double strand DNA
single strand binding proteins prevent strand re-association during replication
Primase generates free 3' end
leading strand continuous 5' to 3' - starts with a primer - DNA polymerase III makes a 5' to 3' strand - continues until template is complete
lagging strand synthesizes 5' to 3' in fragments - primase and then RNA primer - DNA polymerase I removes primer and DNA ligase seals the gap
okazaki fragment the fragment produced by the lagging strand in replication
telomerase solves problem of shrinking DNA due to primers at the end of a lagging strand
transcription DNA ----> RNA - certain codons signal for start and end of transcription -RNA polymerase works like DNA polymerase but does not need primer
one gene on enzyme hypothesis enzymes and genes have a one to one relationship
flow of genetic information DNA --> RNA by transcription RNA --> polypeptide by translation one gene - one peptide
RNA (ribonucleic acid) Polyribonucleotide • Ribose instead of deoxyribosesugar • Phosphate • Nitrogenous bases –C, U, A, G. - U instead of T
codon base pairs of 3 to bridge the language gap during translation - can be redundant (uuu and uuc) both go Phe
RNA polymerase quaternary structure - opens up DNA helix -initiates synthesis with NTP -DNA closes behing - termination
promoter - Promoter = Controlling point for gene expression - Every gene has promoter, usually different. - Start point
transcription factors (TF's) - Proteins that bind to promoter - Different promoters require different TFs - Availability of TFsdetermines gene expression
elongation RNA strand joins in a bubble of an unwinding DNA strand
transcription termination RNA transcript and polymerase fall off and DNA returns to helix structure RNA is a single strand molecule complimentary to the DNA molecule -caps are added to strand for ribosome attatchment
introns and exons introns are spliced out of the RNA strand and the exons are joined together
pre-mRNA RNA strand before the introns are spliced out
mRNA RNA strand with caps on end and introns spliced out
RNA splicing mechanism protein snRNA + other proteins --> spliceosome - intron is cut out
components of translation - mRNA - tRNA - amino acid - Aminoacyl-tRNA synthetases - ribosomes
tRNA - decoder -anticodon corresponds to a specific amino acid -anticodon complimentary to codon
Aminoacyl-tRNAsynthetase (AARS) enzyme that catalyzes bond formation between tRNA and amino acid - assures accuracy - 20 different synthetases for different amino acids and tRNAs
wobble relaxed base pairing - some tRNAs recognize multiple codons
ribosomes two subunits - RNA + proteins - provide physical site for translation -have multiple functions
translation processes 1.) Initiation 2.) Elongation 3.) Termination
Initiation of translation -small sub unit of ribosome -mRNA -initiator tRNA
Elongation of translation -transfer of a peptide back to "A" adds one amino acid to the chain -goes back to "P" with translocation - goes back and forth until chain is complete
termination of translation release factor recognizes stop codon (UAG,UUA, OR UGA) -polypeptide is released with GTP
polyribosomes (polysomes) - multiple ribosomes can be on a single strand of mRNA
mutation - Changes in the genetic material - Chromosome changes 50% of spontaneous abortions - Down syndrome (extra chromosome 21) - Smaller changes in DNA Uncorrected errors in replication Caused by mutagens
mutagen agent that causes mutations ex.) Radiation and chemicals
effects of mutation (1) mutations cause change in DNA - altered product --> function altered or absent - biological consequences depend on the function of the product (if it's vital or not)
effects of mutation (2) somatic cells vs. germ cells - somatic cell mutations--> disease ex.) cancer - germ cell --> heritable disease
neutral mutation when the change of one base pair does not effect the amino acid built
missense mutation when the change of one base pair changes the amino acid that was supposed to go - may cause problems
nonsense mutation when the change of one base pair changes the codon to a stop codon - causes premature termination - protein fragment is produced --> no activity
frameshift mutation more common than nonsense - when one extra base pair is added or taken away - shifts the codon pairs down one changing amino acid sequence downstream
defense against mutations proofreading during replication -repair -> 100 enzymes - mismatch repair - excision repair
proofreading durning replication DNA polymerase I and III detect wrong bases and replace them with the right ones
mismatch repair during replication fixes mess up if proofreading overlooks it
excision repair thymine dimer(caused by UV) --> endonuclease --> DNA polymerase --> ligase = repaired
metabolism - The totality of chemical reactions in an organism - can be considered as a web of interconnecting energy transformations
biosynthesis anabolic pathways light energy + CO2 + H20 --> O2 + C6H1206
degradation catabolic pathways C6H12O6 + O2 --> H2O + CO2 + energy
energy capacity to cause change - kinetic and potential
thermodynamics study of energy transformations
1st law of thermodynamics conservation of energy - total energy amount remains the same
2nd law of thermodynamics entropy (disorder) increases - total energy same in quantity but not in quality
free energy (G) ^G= G final - G initial
exergonic reaction net release of free energy ^G < 0 - more energy at the start of reaction "spontaneous reaction"
endergonic reaction needs free energy from surroundings ^G > 0 - more energy at the start of reaction "non-spontaneous" cannot occur by itself
closed system can do work when not at equilibrium but stops when equilibrium is reached
open system can do work continuously as long as input equals the output
disequilibrium maintained in an open system when input is equal to output
chemical work driving endergonicreactions such as the synthesis of polymers from monomers
transport work pumping substances across membranes against the direction of spontaneous movement
mechanical work beating of cilia, contraction of muscle cells, movement of chromosomes
energy coupling I production of glutamine is endergonic and non-spontaneous - but when paired with production of ADP and P the overall process is exergonic and is spontaneous
energy coupling II glutamatic acid + NH3 is endergonic but is spontaneous when paired with ADP and P reaction
ATP hydrolysis ATP turns into ADP and P releasing free usable energy
ATP synthesis ADP +P + energy from catabolism --> ATP
glucose - model food molecule - plants and animals use polymers of glucose for energy storage -Glucose + O2 --> CO2 + H2O + free usable energy
glycolysis glucose --> pyruvate - takes place in the cytosol - energy investment phase (2 ATP) - energy pay-off phase (2 pyruvate, 2 ATP, 2 NADH)
NAD+ another major player in energy transformation - can receive electrons, protons, and energy to become NADH
fermentation 1 yeast cells no oxygen - glucose --> 2 ethanol + 2CO2 + 2ATP
fermentation 2 muscle cells (lactobacter) no oxygen - glucose + 2 ADP + 2P --> 2 Lactate +2 ATP
fermentation continues from glycolysis in absence of oxygen regenerates NAD+ ends with excretion of ethanal or lactate no additional capture of oxidation energy used by red blood cells, micro-organisms etc.
mitochondria compartments two membranes inner membrane in folds called "cristae" matrix inside the inner membrane
citric acid cycle summary Acetyl-CoA (2C) 2 CO2+ 3 NADH + 3 NAD++ FAD ---> + FADH2+ (ATP) + (ADP) + P
ATP yield during respiration glycolysis - 2 ATP citric acid cycle - 2 ATP oxidation - 32-34 ATP
chemiosmosis An energy coupling mechanism that uses the energy stored in a proton-motive force (proton gradient) to generate ATP.
ATP synthase - H+flows from inter- membrane space through synthaseto matrix - Flow rotates rotor, driving conformation changes in catalytic knob subunits - Conformation changes force condensation of ATP + P ---> ATP
what is the reason for differences in complexity? % of gene not coding for protein or RNA - the more complex the organism the greater ----the amount of non coding DNA - number of genes or size of genome do not matter
Genome 1920 by Winkler - gene + chromosome - sum of all information present in a cell
open reading frame from the start codon to the stop codon
high throughput techniques used to study genes 1.) nucleotide sequences of all DNA in the chromosomes of an organism 2.) DNA microarrays- detect all mRNA's transcribed 3.) 2D gel electrophscesis + mass spectroscopy - detect all proteins translated in cell
reductionism study biology by breaking down in to simpler forms assumptions: 1.) know how the simple parts work then you know how the organism works as a whole 2.) what these parts are assembled of --> same characteristics (molecules --> cell)
holism emergent properties - the whole is greater than the sum of its parts ex.) humans have consciousness but single brain cell does not
Network Biology (systems biology) Interactions among the parts are emergent properties - complex systems are a result of networks
nodes the parts of a network system
links the interactions between nodes of a network
interactome interactions between proteins in a cell - lock and key
evolutionary properties of life - growth and development - reproduction -evolution
metabolic properties of life - ordered structure - energy from environment is required - regulation (homeostasis)
metabolic aspect of life all life is an open system - matter and energy in matter and energy out - life is dynamic - turn-over (breakdown and re-synthesis)
why we need to know what "alive" means? - astrobiology (outer-space exploration) - determining death - determining when life starts - maintaining life - self understanding - creating life
why is synthesis of life an important biological goal? - demonstrate our understanding of life - demonstrate the validity of materialism and the lack of a need for vitalistic forces - determine how life got created
mycoplasma - prokaryote (no cell cell wall) - chromosomes are in a circle - smallest free living -pathogens - small genomes (500-1000 Mbasepairs)
Venter (biologist) worked with mycoplasma to synthesize life
positive control chemically synthesized the entire genome - computers tell robots the sequence
protein aggregates - proteins and nucleic acids spontaneously interact (energetically favorable) - also with ribosomes and viruses
possible reasons why complete synthesis has not been achieved - macromolucular parts must assemble in certain order - templates (templates must form to create other molecules)
Created by: Lindquist
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