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BIO 130 MIDTERM

bio 130 midterm memorization

definition of cell The fundamental unit of life
3 scientist who formulated cell theory Schleiden, Virchow and Schwan
cell theory 1. all living organisms are made up of 1 or more cells 2. ever cell is the structural and functional unit of life 3. cells can only arise from pre-existing cells
exceptions to cell theory viruses, viroid's and prions
viruses - need host cell to live - need host cell to replicate - only small nucleic acids covered in protein coat ( no cell structure)
viroid's - small circular RNA ( no protein coat or cell structure) - need host replicate
prions - no nucleic acids - proteinaceous infectious particles
Cell properties 1. Cell membrane 2. Genetic program 3. capable of producing more of themselves 4. Acquire and utilize energy 5. carry our chemical reactions 6. Mechanical activitives 7. respond to stimuli 8. self regulation
cytoplasm ALL contents found inside cell membrane minus the nucleus
cytosol jelly like internal fluid environment of cell ( cytoplasm minus organelles)
gene the DNA code needed to produce a functional product
central dogma flow of genetic information DNA-RNA-Protein
Capable to produce more themselves ability to duplicate genetic material before division
Carry out chemical reactions metabolic pathways, ex; glycolysis
Engage mechanical activities transportation in and out
Respond to stimuli have receptors they can comprehend
Capable of self regulation if not causes this such as cancer
Eukaryotes descended from which domain archaea
Prokaryotes single celled, no nucleus or membrane bound organelles, single circular chromosomes, rely on cell wall for internal structure, reproduce through binary fission
Bacteria many have plasmids, have cell wall surrounding cell membrane
Archaea isoprenoid cell membrane, live in extreme habitats
Protists mainly single celled, colonies ex: Algae, water molds, slime molds, protozoa
Fungi chitin cell wall, heterotrophs, ex; yeast, rusts, smuts , mildews, molds mushrooms
heterotrophs dependant on preformed organic molecules from energy- absorb directly from the environment
Plants multicell, cell wall of polysaccharide's, vacuoles full water, intercellular connections called plasmodesmata, autotrophs
autotrophs produce their own food, convert suns energy into chemical energy
animals multicell, no cell walls, heterotrophs, early development
Organelles in EMS specialized organelles and structures for cellular activities - nuclear envelope - endoplasmic reticulum ( both) - Golgi apparatus - lysosomes - vesicles - plasma mebmbrane
organelles NOT in EMS mitochondria, chloroplasts, peroxisome's, ribosomes, nucleolus cytoskeleton, centrosomes, cilia and flagella
Model Organism non human species used to understand biology
lysosome contains enzymes to break down organic molecules, pH of 5
cytoskeleton structure on inside of plasma membrane that allows stability ( other organelles attach to it )
peroxisomes enzymes of hydrogen peroxide used to breakdown toxins
nucleus stores genetic information
nuclear envelope protects the nucleus
Golgi apparatus packaging and processing of lipids, proteins and cards
pure element element that contains only 1 atom
orbital can hold a max of 2 electrons
multiple atoms molecules
covalent bonds valence electrons are shared, can be polar or nonpolar depends on electronegativity( if 1 pulls more equals polar)
strongest type bond covalent
Ionic bonds electrons are given, significant difference in electronegativity, creation of ions when dissolved in water split apart
cation extra protons relative to electrons
anion extra electrons relative to protons
Ionic in water when dissolved in water ions are pulled apart and become surrounded by water molecules, hydrogen will associate with the anion ( due to neg charge) and oxygen will associate with cation ( post change)
water chemistry medium of life( most abundant in bio), can dissolve more molecules than anything else, ( universal solvent) Polar,
Hydrogen bond weak bond formed between an electronegative atom and a hydrogen atom that is already covalently linked to another atom , H atoms form H-bonds with highly electronegative atoms ( N, O , F)
pH the measurement of concentration of proton's in a solution
enzyme rules - highly specific - required specific pH - Lower the activation energy as a catalyst - fit substrate - proteins
organic molecules contain carbon
Organic molecules proteins, nucleic acids, carbs, lipids
which organic molecules is not a polymer lipids
condensation reaction monomers combine with each other to from covalent bonds and water molecules are released as by-product, requires energy
hydrolysis polymers are broken down into monomers and water is inserted across the bond
organic molecule with largest variety of functions proteins
proteins functions - enzymes - transport - cell signalling - movement - support - defense
physiological pH 7.4
zwitterion a polypeptide that contains an equal number of positive and negative functional groups and net charge is 0
peptide forms carboxyl releases a oxygen atom and the nitrogen loses two hydrogen atoms to produce water
nucleic acids encode genetic information in the sequence of nucleotides. DNA and RNA are polymers of nucleotides
structure nucleotides nitrogenous base ( 2 types) , 5 carbon sugar, one or more phosphate group
2 types of nitrogenous bases pyrimidine: base that contains single ring ex: cytosine, thymine and uracil purines: base contain double rings ex: adenine and guanine
nucleoside only a sugar and base no phosphate
nucleotides 3 parts, import cell signals ex: AMP or cAMP, cleave of phosphate in to release energy, act as coenzymes/factors,
coenzymes/ factors organic non protein molecules needed for enzyme functions. ex: adenine-containing nucleotides combine with vit. B, or Nicotinamide ( Vit. B3 adenine dinucleotide)
connection of nucleotide's forms DNA and RNA through phosphodiester bonds
directionality of RNA and DNA formation of the polypeptide bond in between 3 prime on sugar and phosphate. start is called 5 prime and nucleotides are added to the 3 prime end
how is DNA and RNA built 5 prime to 3 prime
nucleoside only a sugar and base no phosphate
carbohydrates ratio 1:2:1 of c h and o
nucleotides 3 parts, import cell signals ex: AMP or cAMP, cleave of phosphate in to release energy, act as coenzymes/factors,
coenzymes/ factors organic non protein molecules needed for enzyme functions. ex: adenine-containing nucleotides combine with vit. B, or Nicotinamide ( Vit. B3 adenine dinucleotide)
connection of nucleotide's forms DNA and RNA through phosphodiester bonds
directionality of RNA and DNA formation of the polypeptide bond in between 3 prime on sugar and phosphate. start is called 5 prime and nucleotides are added to the 3 prime end
monosaccharides and functions Glucose: photosynthesis and CR Galactose: dairy products Fructose: sweetener
how is DNA and RNA built 5 prime to 3 prime
oligosaccharides few sugars linking together
carbohydrates ratio 1:2:1 of c h and o
disaccharides sucrose- table sugar
functions carbs energy source and structural molecules
sugars and proteins glycoproteins
simplest carbohydrates saccharides contain 5-6 carbons and linear or cyclical
sugars and lipids glycolipids
what form carbs normal exist cyclical as more stable, less reactive and easier to break off
polysaccharides lots of sugars together, long term energy ex: starch
monosaccharides and functions Glucose: photosynthesis and CR Galactose: dairy products Fructose: sweetener
how become cyclical carbon in the aldehyde or ketone group forms covalent bond with oxygen of the hydroxyl group
oligosaccharides few sugars linking together
disaccharides sucrose- table sugar
sugars and proteins glycoproteins
sugars and lipids glycolipids
polysaccharides lots of sugars together, long term energy ex: starch
molecules that contain carbon organic molecules
membrane functions compartmentalization selectively permeable transporting scaffold for activities responding to signals intracellular interactions energy transduction
glycolipids crab with a lipid attached
glycoprotein car with protein attached
cell membrane components carbs, lipids and proteins
micelles spheres that form when a phospholipid head is too big and bulky and the 1 hydrophobic tail is buried
bilayer smaller heads and 2 hydrophobic tails
liposome added test tube of water and spontaneously form enclosed bilayers, most effective, self healing and will spontaneously rearrange themselves
membrane features dynamic, continuously moving, forming and reforming
affects of fluidity length tails, double bonds and cholesterol
Length tails on fluidity longer the tail the less fluid
double bonds on fluidity less double bonds is less fluid. mor double bonds more fluid
cholesterol on fluidity inserts into the bilayers. can control fluidity dependant on the temperature " buffer" if cold. cholesterol will be more fluid and if hot cholesterol will be more solid . amphipathic in nature
lipid rafts specialized microdomains that serve as platforms for various cell processes, moves laterally, allows to be dynamic and specific functions
integral protein permanetly associated with the membrane and can span the entire lipid bilayer they are transmembrane
peripheral proteins temporarily associated with membrane via covalent bonds. can be cytoplasmic ( in cell) or extracellular( out cell)
membrane proteins functions transporters receptors enzymes anchors
membrane carbs always face outwards, covalently linked to either a protein or lipid ( glycoprotein and glycolipid.
endoplasmic reticulum synthesis of lipids and protein's, largest organelle, network of interconnected tubes and flattened sacs , lots SA from highly folded nature
Golgi apparatus modifies proteins and lipids produced by the ER, acts as a sorting station
lysosomes enzymes that breakdown all macromolecules
mitochondria specialized organelles that harness energy for the cell
cytoskeleton protein scaffold that provides cell structure
plant cell contains all but also cell wall( support) vacuoles ( turgor's pressure) chloroplasts ( convert energy into sunlight)
Do all cells have a cell membrane FALSE
Endomembrane system eukaryotic cells with internal organelles that are surrounded by membranes that interact together physically or through vesicles
why have endomembrane system allows specific functions to take place within defined spaces of the ell
organelles in the EMS plasma membrane and nuclear envelope ER and Golgi apparatus lysosomes vesicles
inner most organelle of EMS nucleus
nucleus a double membrane, inner and outer. has nuclear spores for molecules to travel in and out, spores give communication with rest cell
nucleus to ER nuclear membrane is physically continuous with the ER
lumen the interior space of the flattened sacs in ER
rough ER ribosomes attached- protein synthesis can also be free floating
smooth ER no ribosomes, produce vesicles to move freely, site of fatty acid and phospholipid synthesis lots of SER are specialized to lipid production
golgi apparatus - further modify proteins and lipids from ER - sort proteins and lipids to move to final spot - add carbs to proteins or lipids
cisternae flattened sacs i Golgi apparatus, surrounded by small vesicles which transport proteins from the ER to the Golgi and Golgi to cell
glycosylation ex of enzymes in Golgi, all performed in different region and very specific. this is process of carbs covalently linked to lipids or proteins or aa
lysosomes specialized vesicle from GA, has proton pump to keep pH 5, recycle unneeded macromolecules
membrane organelles not in EMS mitochondria and chloroplasts
smiliarity in mitcon. and chloro. specialized in harnessing energy and semi autonomous
semi autonomous grow and multiple independently and contain their own circular genomes
mitochondria create ATP, rod shaped,
outer membrane mitochondria integral proteins that are porins
inner membrane mitochondria highly convoluted ( twisted and folded) this has ETC and ATP synthase
intermembrane space aqueous compartment between the 2 membranes
matrix kerbs cycle, ribosomes and DNA
chloroplasts where photosynthesis occurs, suns energy to make simple sugars, double membrane
thylakoid internal membrane bound compartment, light collecting pigments ( chlorophyll) which makes green. flattened sacs
lumen space inside thylakoid
grana orderly stacks of thylakoids
stroma space surrounding thylakoid
origin chloroplasts and endosymbiotic relationship between and cyanobacterial cell that had been engulfed by a eukaryotic cell
origin of mitochondria free living bacteria, originated as endosymbiotic bacteria - proteobacteria
theory 1 eukaryotic cells started from ancestral archaeon and later incorporate the proteobacterial cell
theory 2 eukaryotic cells evolved from symbiosis between archaeon and proteobacteria
movement into cell influx
movement out of cell efflux
net flux when 1 exceeds the other - one more dominant
passive transport no energy required, driven by concentration gradient ; simple and facilitated diffusion - nonpolar molecules, small unchargered polar
facilitated diffusion down conc. gradient, carrier and channel protein
carrier protein specific molecule binds to transporter, triggers conformational change to protein, molecule now exposed to opposite membrane surface and diffuses down concentration gradient
channel protein integral proteins, selectively permeable, some have gated channels
osmatic pressure the tonic of the solution
crenation hypertonic situation in animals where cells shrivel and die
plasmolysis hypertonic situation in plants pull away cell wall and die
hemolysis animal red blood cell burst due to hypotonic state
turgid turgor's pressure in plants due to hypotonic state
active transport movement against concentration gradient, requires energy, protein carrier
sodium potassium pump 3 na out 2 k in
ATPase the transport protein to move na out and k in
electrochemical gradient energy stored in concentration gradient from primary active transport, both electrical and chemical component drives secondary active transport
secondary active transport movement of molecules against their gradient due to the electrochemical gradient from active transport
antiport 2 solutes move in opposite directions
symport 2 solutes move in the same direction
exocytosis vesicle fuse with the cell membrane, to move out, budded from EDMS, meets membrane and re fuses emptying contents to extracellular space
endocytosis material outside cell brought into cell through vesicle that can fuse with other organelles. cell membrane makes the vesicles and pinches off
invaginates forms a pocket around the target material
phagocytosis uptake of particle matter, this is the delivery to a lysosome via phagosome. phagosome and lysosome fuse to make a secondary lysosome - actives lysosomal hydrolic enzymes, contents are digested in secondary lysosome
benefits of phagosomes nutrition defense ( macrophages and neutrophils) and enzymes
pinocytosis cell drinking, extracellular fluid taken without recognition, not merge with lysosome
receptor mediated endocytosis receptor proteins for specific substances, very percise
coated pit site where receptors are concentrated- the indented surface
clathrin attached to the cytoplasmic side, brings vesicle into cell ad delivered to endosomes
endosomes network of tubes and vesicles, early= by peripheral region late= interior part of cell
virulent ability to cause disease
DNA is read 5 prime to 3 prime or 3 prime to 5 prime, typically always 5 to 3 if not specified
DNA grows in the 5 prime to 3 prime end
bases are added to the 3 prime end
hydroxyl group ionization 2 negative charges on the phosphate group at cellular pH
difference of 5 prime to 3 prime end polarity
percentage c=g a=t
which direction does DNA coil to the right to allow other molecules to interact
features of DNA double strand, helix shape, antiparallel, outside contour are grooves
A T
C G
purines Adenine and Guanine
pyrmides Cytosine and Thymine
Bond of A and T two hydrogen bonds
Bond of C and G three hydrogen bonds
Stability of DNA large number of h bonds base stacking ( interaction between bases ontop of eachother)
Why h bond beneficial allows it to be undone easily
Genome the genetic material of an organism
Housekeeping genes genes that are always expressed
gene unit of heredity affecting one or more traits of an organism, a DNA sequence that corresponds to a specific protein
Gen expression production of a functional gene product such as protein
Transcription DNA into RNA
Translation RNA into a protein
Central Dogma in EUK location in nucleus and translation in cytoplasm
Central Dogma in PROK location no nucleus so all occurs in cytoplasm
5 prime end of DNA monophosphate
5 Prime end of RNA triphosphate
RNA features - single stranded - Uracil - Triphosphate - polarity - shorter - more complex shapes - less stable - ribose sugar ( hydroxyl on 2 c)
DNA features - x2 starnded - helical - thymine - longer - more stable - deoxyribose - monophosphate
Transcription enzyme RNA polymerase
direction of polymerase, which end added to 3 prime to 5 prime, added to 3 prime end
direction RNA grows 5 prime to 3 prime
DNA template strand is read in 3 prime to 5 prime
bacteria initation mediated by sigma protein, 1 protein
General transcription factors 6 proteins that work together to initiate transcription. bind to promotor region
transcriptional activator proteins bind to enhancer sequence to recruit RNA pol 2
Protein required to start transcription P v E P: 1 E: 6
initiation of transcription in EUK the looping of DNA so that the activator proteins come into contact with the general transcription factors proteins
RNA bubble is 14 base pairs long
RNA - DNA duplex in bubble 8 pairs long
steps of initiation - General factors bind to TATA box - Activator proteins bind to enhancer sequence - RNA pol 2 binds to TATA box ( GFS) - DNA loops so that activator proteins come into contact with General transcriptional factors creating the Mediator Complex
Process of polymerization reaction - RNA pol 2 detects incoming nucleotides - orients the OH on 3 carbon - O of 3 carbon attacks the innermost phosphate group on nucleotide, provides energy for reaction breaking of 2 phosphates
pyrophosphates 2 incoming phosphates that are released
primary transcript the RNA strand that comes off of the DNA template, it has the information to direct the ribosome to translate the protein
Termination PROK is the mRNA strand doesn't need to be modified as already in cytoplasm
Polycistronic mRNA mRNA that codes the information for more than one gene
Termination in EUK need to be modified so can move out of nucleus safely, Addition of a 5 prime cap, removal of introns and addition of poly A tail
5 Cap added to 5 prime end, a unique 5 to 5 bond, needed so the ribosome can recognize mRNA, protection
Poly a tail 250 Adenines added to the 3 prime end, transcription termination sequence, protection
mRNA splicing removal of introns ( not expressed) and keeping exons( are expressed)
alternate splicing a single gene can produce many different but related protein in different cells as different splicing
amino acids can be charged at physiological pH ( amino and carboxy groups)
hydrophobic AA folded to interior of protein, R groups will aggregate together because of Weak van der Waals forces adding to stability
hydrophilic AA R groups interact with each other or with water, via H bonds, found on outer surface of proteins
Basic AA Positively charged
Acidic AA Negatively charged
Special AA glycine, proline, cysteine
Glycine The R group is hydrogen, no asymmetrical, small and non polar , free rotation around alpha carbon to nitrogen bond, increases polypetides flexibility
proline R group links back to amino group restriction over C-N bond limits amount of protein folding
Cysteine R group contains SH - allows two cysteines to have a disulfide bridge ( very strong covalent bond) - this bridge can connect different parts of the same protein or different proteins together
C terminus free carboxy end of peptide
N terminus free Animo acid end of peptide
synonymously polymer of AA connected by amino acids is a peptide with protein
protein conformation three dimensional structure of a protein
Primary structure linear sequence of AA, determine shape of the next 3 structures
Secondary structure Alpha helix and Beta sheet, results of H bonding between neighboring AA, between FUNCTNYL GROUPS NOT R GROUPS fixed configuration of the polypeptide backbone
Alpha Helix very stable, right handed to allow other molecules to interact with each other, form due to H bonds on the 4th AA amino group above or below a AA carboxyl group
Beta Sheet pleated folding, H bonds , side by side ca be parallel or anti parallel
Tertiary structure conformation of entire protein
Tertiary folding depends on - spatial distribution of hydrophobic and hydrophilic R groups - Chemical bonds ( H bonds, ionic bonds, disulfide bonds)
Tertiary structure determines areas of protein that will form active sites for enzymes exterior R groups that will affect how protein interacts with others
Quantary Structure many proteins of multiple subunits
Homodimer two identical subunits
heterodimer two independent subunits
heterotrimer 4 subunits split in 2- 2 identical
Ribosomes structure RNA and protein, large and small subunit
Euk ribosomes larger than Prok TRUE
A site Aminoacyl RNA
E site Exit
P site peptidyl site
Ribosome moves down RNA 5 to 3
Codon nucleotide combination the specifies the placement of an AA
tRNA contain 70-0 nucleotides, bonds with itself to form base pairs, cloverleaf structure
Where AA attach to tRNA 3 prime hydroxyl site
anticodon 3 bases in the anticodon loop
How attach AA to tRNA specific AA are connected by specific enzymes called aminoacyl tRNA synthetases
tRNA without AA uncharged
tRNA with AA charged
tRNA to mRNA connection the anticodon of tRNA will pair with the start codon of mRNA first because they are antiparallel
64 codons 20 AA, very redundant or degenerate
bases on mRNA are read 5 to 3
Translation Initiation in EUK : initation complex starts at 5 prime cap. than initiation factors get the small ribosomal subunit and the tRNA for methionine and scan for the AUG codon, once reached large ribosomal unit attaches and initiation factors are released
Translation elongation - tRNA and Met enter A site - Ribosome shift to the right 1 codon - Met in P site while ne tRNA in A site - due to orientation the Met reacts with new AA and forms a peptide bond - ribosome shift kicking old tRNA out and bringing charged tRNA in
which direction does the ribosome shift in translation right
Translation Termination - stop codon is reached - protein release factor binds to A site at stop codon breaks bond to polypeptide - creates C terminus
Shine Dalgarno Sequence In prokaryotes, no 5 prime cap so this is the initiation complex, on all mRNA which allows mRNA to code form numerous polypeptides
Affects to Protein Synthesis - DNA accessibility - RNA processing - Transcription factors - post translational modifications ( phosphorylation)
Protein sorting No signal: stay in cytosol Amino terminal Signal: Chloroplast or Mitochondria Internal signalling: nucleus
How proteins sent to ER - Signal sequence on growing polypeptide which causes to be halted by SRP - SRP binds to ER membrane - SRP detaches, process begins again pushing new protein into channel in ER - protein Get packaged into a lumen to be brought out of cell
How proteins anchored to ER - embedded in ER as it is synthesised - ER channel releases into the membrane ( lumen) - once completed protein stays in the membrane
Created by: Mr. Box
 

 



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