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the study of structure, function, behavior & evolution of cells at a molecular level |
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the structural & functional unit of life |
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What do all cells use to transcribe info? |
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what reads each codon & converts information to a specific amino acid |
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what do all cells use as catalysts? |
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what is free energy used for? |
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to create bioogical order among living cells |
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main source of energy for living orgsanisms? |
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what are the macromolecules of sugars, amino acids, and nucleotides? |
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polysacharides protiens nucleic acids |
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all cells are at least enclosed by what? |
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two domains of prokaryotes? |
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algae, protozoans, and fungi are all what? |
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What to plant cells have in comparison to animal cells? |
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cell wall, chloroplasts & large vacuoles |
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origin of life from non living matter (primordial soup theory) |
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What is RNA world hypothesis? |
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Short RNAs catalyze & are templates for their own replication were precursors to living organisms. |
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What did the first cell likely look like? |
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Definition
Replicating RNA in a phospholipid bilayer |
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How did metabolism evolve |
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glycolysis, photosynthesis, oxidative metabolism |
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What things make a cell easy to study? |
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Small Easy to grow/raise/isolate Fast generation time ‘Workable’ genetics Good imaging, e.g. transparent Cheap |
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What organisms are best for scientific study? |
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Definition
tobacco mossaic virus, e. coli, sacromyoces yeast, C. elegans, drosophilia & mice, zebra fish, frogs, thaliana (plant) |
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the ability to distinguish objects in small distances appart |
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Describe brightfield microscopy |
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Cell structures seen by labeling proteins & nucleic acids w/ stains & dyes. Fixation |
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what microscopy is ideal for living organisms? |
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DIC, or phase contrast. (clear) |
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describe epiflouresent microscopy |
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flouresent probes label proteins, (live cells) |
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describe confocal microscopy |
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Enhances contrast & detail by removing out of focus light |
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what microscopy can detect subcellular & macromolecular structures? |
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whats the difference between velocity and equilibrium sedimentation |
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seperation based on size and shape, vs. based on buoyant density |
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how does ion exchange chromatography work? |
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Definition
cells are separated based on charge |
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how goes gel filtration chromatography work? |
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Definition
separates ions based on size |
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how does affinity chromatography work? |
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separates ions based on their affinity to other substrates |
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Key Characteristics of Prokaryotes? |
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Definition
usually single celled, no nucleus, cell walls, small |
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a groups of atoms held together by a covalent bond |
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when electrons are donated from one atom to another. |
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what polarity are covalent bonds? |
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what are electrostatic attractions? |
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attractions between oppositely charged particles |
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Definition
electropositive hydrogen attracted to electronegative. (stronger in sraight line) |
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What are van der waals attractons? |
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Definition
change in the electron cloud of a nonpolar atom induces an oppositely polarized dipole in a nearby nonpolar atom. |
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what effect draws together non polar molecules in aqueous solution? |
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Definition
the hydrophobic affect (like oil coming together on top of water |
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what are the simplest lipids? |
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Definition
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part water soluble & part insoluble |
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amino acids link with what bond to become what? |
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Definition
peptide bonds polypeptides |
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nucleotides use what bonds to form what? |
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Definition
phosphodiester bonds nucleic acids |
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Two strands of DNA are held together by? |
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Definition
hydrogen bonds and stacking interacitons |
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What are the functions of nulceotides? |
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Definition
1. subunits of DNA & RNA 2. Chemical energy (ATP) |
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How do cells not break the 2nd law of thermodynamics? |
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Definition
release heat coupled reactions |
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3 examples of potential energy |
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Definition
chemical bond concentration gradients electric potential |
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4 examples of kintetic energy |
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Definition
heat electromagnetic mechanical electric |
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photosysnthesis converts _______ energy to __________ energy |
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Definition
electromagnetic energy potential |
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are ALL chemical rxns reversible? |
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Definition
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Definition
lower activation energy w/o being consumed DOESN't alter chemical products and reactants at equilibrium |
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energetically favorable rxns reduce_____ increase_________ |
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what is delta G at equilibrium in an Exergonic Rxn Delta G =? In an endergonic Rxn Delta G =? |
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condensation rxns are energetically______ 4 examples of condensation rxns? |
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Definition
unfavorable ATP hydrolysis, polysacharide, nucleic acid & protein formation |
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What amino acids are acidic? What's unique about them? |
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Definition
Glu & Asp Hydrophilic, found on outside of proteins. |
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What amino acids are basic? |
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Definition
Argenine, Lysine & Histodine |
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What amino acids are polar & uncharged? what's unique about them? |
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Definition
Asparagine, Glutamine, Serine, Threonine, & Tyrosine hydrophilic, form H bonds, outside proteins |
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What kind of bonds influence protein folding? |
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Definition
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facilitate proper folding of proteins |
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What do disulfide bonds do? where usually found? |
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Definition
stablize protein structure lysosomal & secretory proteins |
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What is mad cow disease caused by? |
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Definition
misfolded protein (prion) which causes formation of protein aggregates. |
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3 general protein structures? |
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Definition
globular, fiberous, integral membrane |
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Where might an alpha helix protein be found? |
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What stabolizes the backbone in a Beta sheet? |
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What is tertiary structure defined by? |
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Definition
interacitions between side chains of amino acids noncovalent bonds & hydrophobic interactions |
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Quatranary struture is a complex of? ex? |
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Definition
multiple proteins hemoglobin |
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Definition
a region that can fold independantly into a compact stable structure. |
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about how many protein domains are there? common potein domains are called? |
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Definition
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proteins or genes that share a common ancestor |
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Arangement of domains is usually lost or conserved? |
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What kidn of activities do proteins regulate? |
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Definition
structure,regulation, movement, catalyst, signaling & transport |
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How do Ligands Bind proteins? |
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Definition
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Specificity: ability of a protein to bind one molecule over others. Affinity: tightness or strength of binding. |
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What are the two models of enzyme/substrate interactions? |
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Definition
lock and key model induced fit (glove) |
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How do enzymes promote catalysis |
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Definition
binds two substrates & makes them change binds substrate to enzyme to create partial - or + rxn strains bound substrate &forces change |
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How is protein synthesis and degredation regulated? |
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Definition
1. rate of mRNA transcription 2. mRNA processing, export & stability 3. rate of translation 4. rate of degradation |
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What determines the lifespan of a protein? |
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Definition
Susceptibility to proteolytic degradation (eliminates misfolded or damages proteins) |
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what molecule degrades proteins? |
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Definition
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what is allosteric regulation |
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Definition
the end product goes to the beginning of the chain & inhibits the chain. |
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Definition
any change in a protein’s tertiary or quaternary structure induced by noncovalent binding of a regulatory molecule (allosteric effector). |
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what does phosphorylation do to protein activity? |
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Definition
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what is atomic weight? Atomic Number? |
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Definition
Atomic Weight = No. of Protons + No. of Neutrons Atomic Number = No. of Protons |
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4 types of macromolecules in a cell? |
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Definition
carbs, lipids, proteins, & nucleic acids |
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glycogen is in _______cells and Starch is in _______cells |
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Definition
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Difference between a nucleotide and a nucleoside |
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Definition
nucleoside = sugar +base nucleotide = sugar + base + phosphate |
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Definition
display of chromosomes at mitosis |
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chromosome: single, linear DNA molecule with associated proteins that pack DNA into a more compact structure chromatin: complex of DNA & protein |
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Definition
pseudogene: duplicated gene inactivated by mutation |
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what is essential for chromosome duplication? |
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Definition
Centromere, replication origins & two telomeres |
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what is the structural unit of chromatin what do they contain? |
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Definition
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what are nucleosomes made of? |
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Definition
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helps pull nucleosomes into 30 nm fiber |
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what phase of chromosomes contain regions of euchromatin & heterochromatin? |
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Definition
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Euchromatin:
Heterochromatin: |
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Definition
euchromatin: ‘transcriptionally active’, open, decondensed heterochromatin: ‘transcriptionally inactive’, closed, condensed |
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How does DNA become accessible? |
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Definition
Chromatin-remodeling complexes use energy from ATP hydrolysis to move nucleosomes & decondense chromatin. |
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At what step can gene expression be regulated? |
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Definition
transcription RNA processing RNA transport mRNA degredation translation protein activity |
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What is the most important regulatory mechanism in genes? |
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Definition
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What makes RNA from a DNA template? |
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Definition
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3 steps of transcription in bacteria? |
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Definition
initiation elongation termination |
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What do repressors do? activators? |
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Definition
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Two parts of transcriptions activators? |
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Definition
DNA binding domain + activation domain |
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Wht is passive repression? |
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Definition
Repressors can compete with activator for same DNA binding site |
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Where is the control region in most eukaryotic genes? |
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Definition
Control region includes promoter (where Pol II & general transcription factors assemble) & regulatory sequences. |
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What does a DNA binding Domain do? Activation Domain? |
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Definition
Recognizes a specificity DNA sequence |
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How can inhibitors inhibit transcription? |
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Definition
interacting with Mediator, general transcription factors or corepressors |
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What do HATs Do? What to HDACs Do? |
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Definition
activate transcription by adding acetyl groups repress it by removing them |
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does DNA methylation turn genes off or on? |
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