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Biology 111

by: Alanna M

Biology 111 BIOL 111 - 02

Alanna M

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Study guide covering material on exam #1 including notes from study session on Friday.
Bio I: Cells, Genetics, Development
Dr. Kolber
Study Guide
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This 8 page Study Guide was uploaded by Alanna M on Sunday September 11, 2016. The Study Guide belongs to BIOL 111 - 02 at Duquesne University taught by Dr. Kolber in Fall 2016. Since its upload, it has received 11 views. For similar materials see Bio I: Cells, Genetics, Development in Biology at Duquesne University.


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Date Created: 09/11/16
1 Biology Exam #1 September 16, 2016 Dr. Kasey Christopher, Section 2 Chapter 1: Scientific Method: - Know the order of the scientific method - Be able to determine control versus experimental as well as variables Order of Scientific Method: 1. Observation Something you have a question about, want to know more about, or just want to experiment about. 2. Question What is it you want to learn? 3. Hypothesis Educated guess 4. Test/Experiment Design an experiment and test hypothesis 5. Conclusions Checking data and comparing it to hypothesis. Either your hypothesis is supported or not supported (where you can reject hypothesis) *Replication: repetition of an experiment to improve accuracy of results. What is a theory? Many experimental conclusions that lead to a theory Independent Variable: Variable you have control over, what you choose to manipulate Dependent Variable: What you measure in the experiment, what is affected in experiment Experimental Group: Group that receives the independent variable Control: Part of the experiment where the independent variable is not included, not getting experimental change Chapter 2: The Molecules of Life: - Periodic Table - Bonds General structure of atoms… Dense core – composed of protons and neutrons [has a positive charge] Energy shell – space electrons travels [has a negative charge] Valence shell – outer shell [typically can hold 8 electrons except for first row elements] What does the atomic number of an element tell you? 2 The number of protons in the element. This also tells you the number of electrons in the element. Number of protons = number of electrons The row of the element tells you the number of energy levels The column of the element tells you the number of electrons in the valence shell Carbon Atomic number: 6 Protons and electrons: 6 Row: 2 Energy levels: 2 Column: 4 Valence electrons: 4 4 Types of Bonds: Covalent Polar Covalent Hydrogen Ionic Covalent – pair of valence electrons shared between two atoms H H Polar covalent – unequal sharing of valence electrons δ- Water Molecule δ+ δ+ Hydrogen bonds – hydrogen bound to an electronegative atom is attracted to an electronegative atom of another molecule [between molecules] 3 Ionic bonds – strong attraction between two oppositely charged ions Ions: atoms that lose or gain electrons Between high electronegativity and low electronegativity Polar Hydrogen Bonds Hydrophilic States of matter Hydrophobic Cohesion Hydrophilic – polar, ionic compounds, soluble in water, like being happy in water Hydrophobic – non polar, insoluble in water, hate being in water (“phobia” of water) *Hydrogen bonds influence structure of water in liquid state, the water molecules have movement, making and enhancing hydrogen bonds, denser than ice. In solid state, the water molecules don’t have movement, hydrogen bonds are maximized, less dense than liquid. Isomers – structural diversity of carbon based molecules Organic molecules: - Carbohydrates - Lipids - Proteins - Nucleic acids Carbohydrates Source of energy Carbohydrates are saccharides Carbon and water = carbohydrates Two types of saccharides: monosaccharides and polysaccharides Monosaccharides: simple sugars. Six carbon sugars, almost all in ring form. Metabolized quickly, don’t give a lot of energy. For example, glucose and fructose. Polysaccharides: starches (like glycogen), branches glucose; long term storage of energy in liver. Release energy slowly, long term source of energy. Lipids Fatty acids Triglycerides Hydrophobic Steroids Phospholipids Fatty Acids Palmitic acid: carboxyl group attached to hydrocarbon chain. Very hydrophobic tail 4 Saturated fatty acids Carbons saturated with hydrogens, solid at room temperature, densely pack with each other due to Van Der Waals forces *Van Der Waal’s Forces: due to constant movement of electrons, there are transient charges. When in close proximity, charges attract. Things that happen between non-polar stuff Even weaker than hydrogen bonds Unsaturated fatty acids They have kinks, liquid at room temperature, double bonded carbon Trans fats Unsaturated, double bonds do not form kinds, force hydrogen onto unsaturated Triacylglycerol Long term storage of energy Steroids Cholesterol is a steroid Core of 20 atoms into four fused rings Phospholipids ½ hydrophobic polar head group hydrophobic tail make up cellular membranes 5 Proteins are composed of amino acids chains of amino acids acids linked by peptide bonds polypeptide bonds one amino acid = residue Chapter 3: - Frederick Griffith Experiment - Avery, Macleod, McCarty - Nucleic Acids - RNA transcripts - Functions of different pieces of transcript Frederick Griffith Experiment: Know conclusion: information molecules allowed non-virulent bacteria to get transformed to virulent bacteria. Avery, Macleod, McCarty Know hypothesis and conclusion Hypothesis: transformation of bacteria will not occur if information molecule is removed Conclusion: removal of DNA using DNase did not result in transformation, DNA is the information molecule. If I get rid of transforming factor, I can’t transform. Destroy DNA with DNase can no longer translate bacteria. Nucleic Acid Information molecules Chemically how we transfer information cell to cell Basic structure: phosphate, sugar, and base Has a base on 1’ (one prime) carbon, phosphate on 5’ carbon. Phosphodiester bond between 3’ –OH and 5’ phosphate of next nucleotide Nucleic acid direction is 5’ to 3’. - Know how to get RNA transcript from non-template strand o In non-template, basically the same except T -> U. start with 5’. - Know how to get RNA transcript from template strand o In template, start with the END (b/c antiparallel) so 5’ -> 3’, start with 3’ end. G- >C, T -> A, A -> U, C -> G 6 *always give answers starting with 5’ end Normal Function Activator Binds to enhancer and recruits mediator Enhancer Bound by activator, helps transcription happen RNA polymerase Actual enzyme that accomplishes transcription, links to RNA, 5’ to 3’ direction Promoter Start site for transcription, where RNA needs to bind to transcribe Terminator Where transcription ends Transcription Factor Binds promoter and recruits RNA polymerase Chapter 4 - mRNA - tRNA - Translation - Proteins and their structure mRNA Codon that is specific for AA (amino acids) rd The 3 base is redundant AUG is the start codon tRNA attachment site for amino acids anti codon 20 different aminoacyl tRNA synthetases for each amino acids Translation “Initiation factors” detect 5’ cap of the mRNA AUG is the start codon (methionine) first amino acid Stops at stop codon Ribosome Introns to get rid of Extrons to get keep 7 Treat different things as introns versus extrons. 4 segments of DNA above. Doesn’t mean from same transcript you can make however many you want. Normal Function Transcript Protein Spliceosome Splices; getting rid of Too long, would keep Too long, get introns introns screwed up. Could be too short 5’ cap Initiates translation Unstable but wouldn’t see huge difference in length Polyadenylation stability shorter Probably get made? Translation initiation Bind to mRNA (5’ factors cap) recruit ribosomes and recruit first tRNA bound to methionine Translation Provide nergy for Methionine elongation factors peptide bonds Translation release Stop codon and Wouldn’t stop factors breaks bond translation, protein between tRNA and would continue to be polypeptide and made and eventually release so protein is get stuck to ribosome done Proteins Amino acids Carboxyl group R group Hydrophobic on inside Connected by peptide bonds between carboxyl group and amino group Know alpha helix and beta sheet difference Protein Structure Primary – amino acid sequence linked by peptide bonds and has specific n-terminal to c- terminal direction Secondary – hydrogen bonds between local regions of backbone. Alpha helix and beta sheets Tertiary – R group interactions. Gives 3D shape. Van der Waals, hydrogen bonds, ionic bonds, and di-sulfide bridges involved 8 Quaternary – not always present, 2+ polypeptide chains, not a requirement. Linked using any possibilities.


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