Review for Exam 1
Review for Exam 1 BIOL 3510
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This 11 page Study Guide was uploaded by Marin Young on Sunday February 7, 2016. The Study Guide belongs to BIOL 3510 at University of North Texas taught by Dr. Chapman in Spring 2016. Since its upload, it has received 269 views. For similar materials see Cell Biology in Biological Sciences at University of North Texas.
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Date Created: 02/07/16
Exam 1 Study Guide | BIOL 3510 Notes by Marin Young □ What technological developmentand subsequent observationsled to the birth of cell biology? • 1665:Robert Hooke saw dead cork cells (plant cell walls) under his early microscopeand coined "cells" to describe little roomslike monks lived in • 1838/1839:Schleiden says plants are made of cells, Schwann says animals are made of cells ○ Schwann cells, which wrap around and insulate long neurons, are named after this Schwann □ What is the cell theory? • idea that all living things comefrom division of existing cells, and cells are "basic unit of life" □ What are the average sizes of cells and organelles and the resolutionlimits of different types of microscopes? • Eukaryoticcells: 10-50 µm • Prokaryoticcells: 1-3 µm Light 0.2 µm •Visible-light microscopy:requires staining and fixing (usually with heat) to see microscopy 200 nm well, or differential interference contrast (like phase-contrast)to see living cells (three types) with optics tricks •Epifluorescent: uses a fluorescent stain to label structures and a UV lamp to cause the dye to emit visible light; best for living cells •Confocal fluorescent: uses a laser beam instead of a UV lamp to illuminate sample, which improvesimage quality by helping focus on a 3-D sample •Remember,the resolution is still 200 nm, but focus depends on sample thickness; you've probably run into this problem in labs where you can't see an entire object in focus at the same time (I'm thinking of diatoms, for anyone who took micro) Scanning 20 nm Specimen coated with a thin layer of heavy metal like gold and blasted at an electron angle with a beam of electrons, which bounce off the metal and onto a detector. microscopy A connected computeruses the electron pattern to determine structure based on angles of "reflection" where electrons bounced. Transmission 2 nm This is a lot more like light microscopywith electrons instead of light: a condenser electron focuses electrons on a thin sample, which can be stained with electron-dense microscopy chemicals like uranium acetate or lead citrate. Some areas absorb moreelectrons than others. The electrons go through electromagneticobjectiveand projector lenses and hit a detector screen to make a digital image. □ Compare and contrast different types of light microscopyand electron microscopy. • See chart above! □ What do images produced by the different types of microscopylook like? (Check out the relevant figures in your book). Visible-light microscopyusing stains From <https://upload.wikimedia.org/wikipedia/commons/1/ 15/Cilia_light_micrograph.jpg> Differential-interferencecontrast From <https://commons.wikimedia.org/wiki/File:S_cerevisia e_under_DIC_microscopy.jpg> Epifluorescence From <https://commons.wikimedia.org/wiki/File:Dyeing_the _reactive_astrocytes_by_using_anti-GFAP_antibodies_ 2.jpg> Confocal fluorescence From http://www.pha.jhu.edu/ ~ghzheng/old/webct/note1_1.files/09_ 019.jpg Scanning electron microscopy (Public domain, accessed via https://en.wikipedia.org/wiki/Scanning_elec tron_microscope#/media/File:Misc_pollen.jp g) Lookslike a photograph of a 3-dimensional metal replica Transmission electron microscopy From https://upload.wikimedia.org/wikipedia/com mons/c/c1/Myelinated_neuron.jpg Lookslike a light micrograph in incredibly high resolution □ What are the differences and similarities between prokaryoticand eukaryoticcells? • Similarities: reproduction, expression of DNA via transcription and translation, phospholipid bilayer cell membrane • Differences: presence or absence of membrane-bound organelles and nucleus, presence or absence of introns, number of origins of replication □ What are the subcellular organelles/componentsand their general functions in cells? What cellular components are unique to plants? • I recommendhttp://facstaff.cbu.edu/~seisen/EukaryoticCellStructure.htm if you need a refresher on this □ Be familiar with the general structure of amino acids, peptide bonds and polypeptide chains (or proteins). • Amino acids: Peptide bond: Amino acids in a peptide are called amino acid residues □ While I don’t expect you to memorizethe amino acid side chains, I do expect you to be able to tell if they are nonpolar, acidic etc if the structure is provide as well as their abbreviations Basic/Positive Lysine Lys Arginine Arg Histidine His Note that all abbreviations are just the first three letters except asparagine, Acidic/Negative Aspartate Asp glutamine, and tryptophan! Glutamate Glu Uncharged and Polar Asparagine Asn Glutamine Gln Tyrosine Tyr Serine Ser Threonine Thr Nonpolar Proline Pro Glycine Gly Alanine Ala Valine Val Leucine Leu Leucine Leu Isoleucine Iso Phenylalanine Phe Tryptophan Trp Cysteine Cys Methionine Met □ What are the four levels of structural organization of protein and what characterizes each level? Protein structure •Primary structure: order of amino acids (Asp- Lys-Gly-Tyr…) ○Determinedby covalentbonds in backbone •Secondary structure: alpha helices and beta pleated sheets ○Determinedby hydrogen bonds in backbone ○An alpha helix has R-groups facing out and 3.6 residues per turn--the carboxyl group on residue 1 accepts a hydrogen bond from the amino group on residue 5 (NCC-NCC-NCC-NCC-NCC) ○Beta sheets are accordion-folded and can be parallel (NCC-NCC-NCC backbone runs the same direction) or antiparallel •Tertiarystructure: folding into actual shapes ○Determinedby noncovalentinteractions (hydrogen bonds, hydrophobic interactions, ionic bonds) plus covalent disulfide bonds between R groups ○Domains are sections of a protein that can fold independently (even without the other sections of the same protein) Gene regions for domains can be spliced together to create new proteins, in the lab or in cells (translocationmutations) •Quaternary structure:interaction of multiple polypeptide subunits ○Some proteins are a single polypeptide chain and don't really have 4 structure ○Proteins can be called homo___mersor hetero___mers The blank is the number (di, tri, tetra) Homo = identical subunits, hetero = different subunits ○Rubisco (a plant protein, most abundant protein on Earth) has 8 large subunits (encoded in nuclear genome)and 8 small subunits (encoded in chloroplast genome) genome) □ What are covalent bonds (both polar and nonpolar)? • Strong bonds involving sharing electrons • In nonpolar bonds, electrons are shared fairly • In polar bonds, electrons are shared unfairly/unequally ○ Some moleculeswith polar bonds are polar molecules □ CH C3 is polar because the side with the Cl has a partial negative charge and the side away from it has a partial positive charge □ CCl 4s nonpolar because the polar bonds all cancel each other out: the outer chlorines have partial negative charges and the inner carbon has a partial positive charge, but there's no partially positive or negative "side" □ What are 4 types of non-covalentbonds/forces relevant to cells? Be able to describe them. • Van der Waals interactions: all atoms are slightly attracted to each other by "induced dipoles" (polarity wobble) ○ This is most important in nonpolar amino acid residues • Hydrophobic interactions: very nonpolar particles stick together to minimize exposure to water (this is why oil and water don't mix • Hydrogen bonds: occur between an oxygen or nitrogen with a lone pair, and a hydrogen on an oxygen or nitrogen--hydrogens on carbon atoms do NOT make hydrogen bonds • Ionic or electrostaticattractions:opposites attract! Positiveand negative charges are attracted to each other □ How do proteins fold? • Domains are independently folding sections that are small enough for noncovalentinteractions to pull the amino acid residues into place • Domains then fit into each other □ What are α helices and β sheets? How are they formed? • Types of secondarystructure formed by hydrogen bonds within the NCC backbone of a polypeptide □ What is a protein domain? What are chaperones? • Domain:independently folding section • Chaperone: protein that helps facilitate correct folding □ What are binding sites, ligands, substrates, active sites, catalysts,enzymes, and allosteric proteins? • Binding site: a region of a protein with a structure adapted for binding to another molecule • Ligand: a moleculesuch as a hormone that binds to a receptor or other protein • Substrate: a molecule that undergoes an enzyme-catalyzedreaction • Active site: a site where a protein's activity takes place (usually also a binding site) • Catalyst: any substance that increases a reaction rate by lowering activation energy without being changed or altering the free energy change of the reaction • Enzymes: biological catalysts, usually proteins but sometimesRNA molecules ○ Can catalyze reactions by: □ holding substrates near each other, □ bending bond angles to help break a bond ("stabilize the transition state"--help form the very middle of a reaction step where one bond is half broken and another is half formed),or □ temporarilyholding "extra" protons or electrons to stabilize an intermediate • Allosteric protein: a protein whose activity is regulated by moleculesbinding at a site besides the active site (like an inhibitor deactivating a protein by binding to a special regulatory binding site) □ How does feedback regulation work? • A product of a reaction or set of reactions inhibits the same reaction(s), usually by allosterically inhibiting an enzyme that catalyzes an earlier step □ What are four ways protein activitiesare modulated in a cell? • Feedback inhibition, phosphorylation/dephosphorylation,degrading ubiquitin-tagged proteins, allosteric regulation, and possibly also controlling the amount of transcription/translationthat occurs □ What do conformationalchanges have to do with protein activity? • Changing the shape of a protein can expose a previously buried active site, movean important catalytic amino acid residue into a useful place, or even get the protein out of its own way--structure determines amino acid residue into a useful place, or even get the protein out of its own way--structure determines function, so changing structure changes function and can turn a protein from on to off □ What are kinases, phosphatases, and GTPases (GTP binding proteins)? How does these regulate protein activity? • Kinases are enzymes that phosphorylate (stick a phosphate group onto) other proteins/enzymes ○ This often activates the target enzyme,but some enzymes are deactivated by phosphorylation • Phosphatases are enzymes that dephosphorylate (take a phosphate group off of) a target protein ○ This is the opposite of what a kinase does--likewise,it deactivates most target proteins but activates some ○ This also usually releases some energy • GTPases bind GTP and then hydrolyze it to produce GDP and P (phoiphate) ○ GTPases, which include the G proteins that work with G-protein-coupledreceptors, often have other functions, and they're active when bound to GTP □ This means they deactivatethemselvesby hydrolyzing GTP • All of these are means of "switching" proteins between on and off, or between one activityand another □ What are antibodies? How are these produced? • Antibodies are small proteins that bind to foreign moleculescalled antigens ○ They're produced in the body by intron splicing and recombinationof domains that have different shapes ○ They're produced in the lab by regularly injecting an animal with the antigen so its immune system produces antibodies against it, and then harvesting the antibodies by drawing blood □ Be familiar with the general structure of nucleotides, phosphodiester bonds, and nucleic acids. • Two thymine nucleotides are shown, with a phosphodiester bond circled in red • Cytosine and guanine form three hydrogen bonds; adenine and thymine form two ○ Mnemonicfor base pairing: AT&T and Cingular, the cell phone companies ○ Adenine and guanine are purines, which means their structures are bicyclic ("PUGA-2") ○ Cytosine and thymine are pyrimidines ○ One purine and one pyrimidine always base-pair to keep width consistent • A DNA double helix has two antiparallel strands in a right-handed spiral with 10 bp per turn ○ Antiparallel: one goes 5' to 3' (has a phosphate at one end and a sugar at the other) and one goes 3' to 5' (sugar at one end, phosphate at other) ○ Minor and major groovesalternate because of the offset between the two strands Proteins to bind to DNA based on this pattern/shape □ Compare and contrast: Purines vs pyrimidines, ribose vs deoxyribose,RNA vs DNA, heterochromatinvs euchromatin. • A purine has two rings and is wider; a pyrimidine has one ring and is narrower • Ribose has an -OH group on the 2' carbon; deoxyribosehas a hydrogen there instead • Heterochromatinis condensed and hard to express; euchromatin is more open and easier to express □ How are these terms related to each other in the context of double stranded DNA?-- hydrogen bonds, complementarybase pairing, anti-parallel, and polarity. How are complementarysequences “written” with complementarybase pairing, anti-parallel, and polarity. How are complementarysequences “written” with respect to polarity (DNA and RNA)? • Hydrogen bonds between bases are responsible for complementarybase pairing • The polarity of DNA means there's a 5' end (the end with the phosphate group, which is attached to the 5' carbon) and a 3' end (the end with the sugar, which has an -OH group on the 3' carbon • Antiparallel means the strands go in opposite directions (moreon this above) □ What are genomes, karyotypes,chromosomes,homologouschromosome,chromatin, and epigenetic inheritance? • Genome: the set of all genetic material in an organism • Karyotype: an image of all the mitoticchromosomesin an organism's genome, dyed different colors with fluorescent molecules • Chromosome:a completeDNA molecule folded into a condensed structure • Homologouschromosomes:a pair of chromosomescontaining the same sequence of genes, with varying alleles because one chromosomecomesfrom each parent (meaning, they're not exactly identical) • Chromatin: the combinationof DNA and proteins (mostlyhistones) that resides in the nucleus of the cell • Epigenetic inheritance: passing down epigenetic ("above the genome") modificationslike methylationor acetylationof certain histones ○ This allows inheritance of gene expression patterns, not just the genes themselves ○ Very important in cell division, since epigenetic modificationsare crucial to determining what genes are expressed in a cell type □ What three general sequence elementsare needed for chromosomereplication and segregation? • Telomere,replication origin, and centromere □ What are the various levels of chromatin organization and what proteins and interactions lead to their formation? • DNA wraps around specialized proteins called histones ○ A histone complex is an octamer with two each of H2A, H2B, H3, and H4 ○ A 147-bp length of DNA wraps twice around each histone complex,with a 50-ish-bp segment of linker DNA between histone complexes ○ Nucleosome= one histone complexplus its wrapped and linker DNA ○ If this "beads on a string" chromatin (DNA + histones) was exposed to a nuclease, the linker segments would be destroyed and yield nucleosomecore particles (histone complexeswith wrapped DNA) ○ Histone proteins contain many Arg and Lys residues (+ charges attract DNA) and are highly conserved among species H3 subunits' tails are most used for regulation • Nucleosomesare packed into 30 nm fibers ○ Histone H1 (NOT part of the octamer)binds between wrapped and linker DNA to hold nucleosomesclose together ○ Histone tails can also interact • 30 nm fibers form 300 nm loops • 300 nm loops are squished and folded together to form a mitotic (condensed) chromosome □ How do DNA binding proteins access nucleosome-wrappedDNA? • The chromatin remodeling complex slides DNA over the histone complex to expose a different segment □ What is the relationship between the amount of DNA condensation and the level of transcription? • More condensation (tighter packing) correlates with less transcription □ What are the main structural componentsof the nucleus? • Nuclear envelope: two concentric lipid bilayers (like two cell membranes,one lining the other) • Nuclear lamina: mesh of intermediate filaments (a type of cytoskeletalfilament) that supports shape of nucleus • Nuclear pores: channels through the nuclear envelope,made of proteins that selectivelyallow certain moleculesto enter or exit ○ Controls when mRNA can leave (only when capped, tailed, and spliced) • Nucleolus: an important biochemical neighborhood in the nucleus where ribosomesare manufactured • Nucleolus: an important biochemical neighborhood in the nucleus where ribosomesare manufactured ○ Ribosomalgenes are transcribed to RNA Some is considered rRNA and will becomepart of the ribosome; some is mRNA and will be transcribed ○ The mRNA exits the nucleus and gets transcribed in the cytoplasm, and then the proteins synthesized re-enter the nucleus ○ The ribosomal proteins and rRNAs are assembled in the nucleolus □ What is a biochemical “neighborhood”? • An area within the nucleus with characteristics that facilitate different biochemical activities, like an area with lots of RNA polymerasethat's good for transcription or an area with lots of spliceosomesfor mRNA processing □ What are characteristics unique to RNA? • Uracil instead of thymine • Ribose instead of deoxyribose • Usually single-stranded and can take on many, many different structures • Sometimeshas catalytic activity (ribozymes) • Sometimescapable of unconventional base-pairing, like two hydrogen bonds forming between an adenine and a cytosine--it's not perfect, but it's better than nothing ○ Stabilizes a structure just enough to still be dynamic ○ Can also allow different widths of base pairs: an adenine-guanine pair would be wider than a usual bp, and a cytosine-thyminepair would be narrower □ What do polymerasesdo? Remember5’ to 3’. • Synthesize a polymer of DNA or RNA in the 5' to 3' direction • This means they read the template strand from 3' to 5' □ What are the main steps in prokaryotictranscription? What is the role of the promoter(-10 and -35 sequences), sigma factor, RNA polymerase,and terminationsequence? • Initiation, elongation, and termination • There are two short promoterregions, one about 10 bp before the origin and one about 35 bp before the origin • The sigma factor binds to both these promoterregions and helps RNA polymerasebind to the DNA • The termination sequence causes RNA polymeraseto stop transcribing and leave the DNA ○ This can happen with or without proteins, but this wasn't covered in class □ What are the main steps in eukaryotic transcription? What are the roles of the promoter(TATA box), general transcription factors (especially TFIID and TFIIH), RNA pol II, and the C-terminal domain of RNA pol II? • Still initiation, elongation, and termination, but a bit more complex • The promoter/TATAbox binds transcription factors ○ TFIID binds to the TATA box • TFIIH phosphorylatesthe C-terminal domain/cytoplasmictail domain of RNA pol II, which activates it □ How are eukaryotictranscripts processed prior to exiting the nucleus? • Introns are spliced out • A methylatedGTP cap is attached to the 5' end, via a triphosphate bridge • The 3' end is polyadenylated (a long tail of 150-250adenosine nucleotides is added) □ What is the role and compositionof the spliceosome? • Made of catalytic RNAs and proteins • Pulls out introns in a lariat (lasso) shape and splices/joinsexons together □ What is the advantage of alternative splicing? • Multiple different polypeptides can be synthesized to express a single gene, depending on the combination and order of exons spliced into the final mRNA □ How is eukaryotic transcription regulated? • Enhancer regions (located upstream/beforethe TATA box and gene to transcribe) bind activator proteins, which help the mediator protein set up the RNA polymerasecomplex ○ Activator proteins bind specifically to the DNA sequence of their enhancer regions • Repressor proteins can get in the way of RNA polymeraseassembly and transcription Repressor proteins bind to the silencer region ○ Repressor proteins bind to the silencer region ○ Note that neither enhancers nor repressors bind to the promoter region; transcription factors and RNA polymerasedo • Transcription is regulated by a complex "team,"with various specialized roles that help in different ways (and somethat instead slow progress, just like teams in real life) ○ Transcription factors, histone modifiers, and the chromatin remodeling complex can all bind to DNA sequences or to the mediator ○ Regulation with many variables or inputs is called combinatorial control and allows fine-tuning the rate of transcription • Some regulatory proteins allow the expression of genes that make other regulatory proteins that allow the expression of genes that do all kinds of other stuff and make more regulatory proteins that…and so forth ○ These are sometimescalled linchpin/keystonetranscription factors ○ In Drosophila (fruit flies), the protein ey is normally expressed in the eye region but can make a replica eye on the fly's leg if expressed in the leg ○ MyoD causes a chicken fibroblast to become a muscle cell line, which is useful for growing flavorless chicken meat in the lab □ What are codons, the genetic code, redundancy, and reading frames? • Codon: group of three consecutive nucleotides in mRNA • Genetic code: each codon corresponds to a specific amino acid • Redundancy: someamino acids are represented by multiple codons ○ But not the other way around--amino acids are a function of codons, if you like math • Reading frames:where each group of three nucleotides starts (123 456 789 vs 234 567 890; like the placement of bar lines to divide measures of music, if you like) □ What are the important structural features of a tRNA? How is it charged? How is the charging checked? • The anticodon loop is complementaryto the mRNA codon • The 3' end carries an amino acid corresponding to the codon complementaryto the tRNA's anticodon • There are two other loops to make an overall clover-shaped or t-shaped structure • A tRNA is "charged" with an amino acid by an aminoacyl-tRNAsynthetase • Charging is checked two ways: the amino acid should fit in the synthesis site and not fit in the editing site of the aminoacyl-tRNA synthetase □ What are ribosomesmade of? What are the roles of the large and small subunit? What are the E, P, and A sites? • Many proteins and several catalytic rRNA molecules • Large subunit catalyzes peptide bond formation • Small subunit binds mRNA • A (aminoacyl-tRNA-binding) site is where a tRNA enters and brings an amino acid into position to bond with the one before it (on the tRNA in the P site) • P (peptidyl-tRNA-binding) site is where the amino acid leaves the tRNA so that the next amino acid can form a peptide bond to its carboxyl group • E (exit) site is where the tRNA leaves without its amino acid • I highly recommendwatching an animation of this process □ What are the steps in translation including initiation, elongation, and termination? What are the roles of the initiator tRNA, MET-tRNA, release factors, and GTP hydrolysis in translation? • Initiation: the initiator tRNA is a methionyl-tRNA;it and some initiation factors bind to the small subunit ○ Then mRNA binds ○ Then the small subunit carries MET-tRNA down the mRNA until they find a start codon (complementaryto the MET-tRNA's anticodon) ○ And THEN the large subunit can bind, with the MET-tRNA ending up in the P site • Elongation: an aminoacyl-tRNAenters the A site ○ Its anticodon is complementaryto the codon facing the A site ○ At about the same time, the newest amino acid forms a peptide bond to the previous amino acid, and the large subunit translocates (movesa bit towards the 3' end of the mRNA) Forming a peptide bond to the previous amino acid requires that previous amino acid to break its bond to its tRNA, which ends up in the E site when the large subunit moves its bond to its tRNA, which ends up in the E site when the large subunit moves The amino acid just added is still attached to its tRNA, which is now in the P site The A site is briefly empty until another aminoacyl-tRNAcomes in ○ The small subunit translocatesas the tRNA in the E site leaves ○ GTP hydrolysis provides the energy for these bonds to form and translocationsto occur Elongation factors like EF-Tu help with this • Termination:a release factor, which acts a lot like an aminoacyl-tRNA,enters the A site and binds to the stop codon ○ When the large subunit translocatesand the last amino acid leaves its tRNA, the release factor ends up in the P site, which causes the ribosome to disassemble and release the new polypeptide □ What do proteasomes,ubiquitin, and proteaseshave to do with protein degradation? • Proteasome:protein complexwith two cylindrical caps providing channels to a protease core • Ubiquitin: attaches to target proteins, recognized by proteasomecaps, causes target proteins to enter proteasome • Protease: responsible for protein degradation by hydrolyzing peptide bonds in the proteins that enter the proteasome'score □ X-ray crystallography? • Make a pure, solid crystal of a protein and shoot X-rays through it • The diffraction pattern can be mathematicallyanalyzed to find atomic structures • This is how Rosalind Franklin (NOT Watson and Crick) figured out that DNA was a double helix □ Nuclear magnetic resonance spectroscopy? • Applying a strong magnetic field to a protein sample causes measurable atomic vibrations in patterns depending on how close hydrogen atoms are to each other • This only works for fairly small proteins--it's the same NMR used in organic chem, and it gets really complicatedreally fast □ Use of antibodies in immunoprecipitationand as moleculartags? • Antibodies for a specific protein will selectivelybind to that protein • This can cause it to precipitate (like agglutination in blood typing), which isolates the protein • If the antibodies are covalentlybound to radioactivelabels or fluorescent dye molecules, they work as molecular tags to visualize protein locations □ Restriction nuclease digestion? • I'm not sure we talked about this in class, but it's a methodof slicing up DNA in a way that leaves "sticky ends" that can anneal to each other • Combining various DNA moleculeswith the same sticky ends can create a big recombinant DNA molecule □ Electrophoresis? • DNA goes in wells at the negative end of the gel and is electrostaticallyattracted to the positive end of the gel • Smaller moleculesmovefaster, so in a period of time, the DNA moleculeswill be spread out over the gel according to their size • Combining this with restriction nuclease digestion allows restrictionfragment length polymorphism, or DNA fingerprinting □ Hybridization and northern and southern blotting? • I'll update this study guide if these topics are covered in class on Tuesday the 9th, but otherwise, I don't believe they'll be tested □ Genomeediting by nucleases? • CRISPR: Clustered Regularly Interspaced Short Palindromic Repeats ○ Basically, this is a thing bacteria have to "train" their nucleases to target virus sequences for chopping up, and molecular biologists figured out how to use this to target specific sequences for opening in a way that lets them insert more DNA • The explanation in the lecture notes is…fun. Rather than try to recap that, I highly recommendthis article: http://gizmodo.com/everything-you-need-to-know-about-crispr-the-new-tool-1702114381 • The video embedded is also nice--here's a direct link to start at the beginning: https://www.youtube.com/watch?v=2pp17E4E-O8 Fair warning: this starts with an overviewof basic DNA structure, so you may want to skip forward a ○ Fair warning: this starts with an overviewof basic DNA structure, so you may want to skip forward a bit (or enjoy the confidence boost from knowing what they're talking about) □ That's all for now! • Congratulations on making it through Dr. Chapman's giant test review!I hope reading this for you is as helpful as making it was for me. Happy studying, and good luck!
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