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Study Guide for exam 2- chapters 5-7 in Intro Biology

by: Hannah Kissell

Study Guide for exam 2- chapters 5-7 in Intro Biology Biol 121-004

Marketplace > San Juan College > Biology, science, and environmental > Biol 121-004 > Study Guide for exam 2 chapters 5 7 in Intro Biology
Hannah Kissell

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Macromolecules, The parts of the cell, and Osmosis and Diffusion. A total of 38 study questions
Dr. Evans
Study Guide
Biology, cells, Osmosis, Diffusion
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This 8 page Study Guide was uploaded by Hannah Kissell on Saturday October 8, 2016. The Study Guide belongs to Biol 121-004 at San Juan College taught by Dr. Evans in Fall 2016. Since its upload, it has received 3 views. For similar materials see Introduction in Biology, science, and environmental at San Juan College.

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Date Created: 10/08/16
Study Guide for Exam 2- October 10 1. Name the four classes of macromolecules Carbohydrates, Lipids, Proteins, Nucleic Acid 2. Describe what a monomer and polymer are Monomer- single unit molecule that can be bonded to other identical molecules Polymer- monomers linked together by covalent bonds 3. List the steps of condensation and hydrolysis reaction and describe what each reaction is used for Condensation Reaction- monomers move and become a polymer, make a covalent bond and form H2O. Forming long chains and is responsible for many biological transformations Hydrolysis Reaction- polymers break into monomers, break covalent bonds and use H2O. Is used for both biological and chemical reactions 4. Name the functions of carbohydrates The main role of carbohydrates is to provide energy and fuel 5. Describe the molecular formula of monosaccharides A 1-2-1 sequence of (CH2O)n, creating a ring in water 6. Describe a polysaccharide, disaccharide, and glycosidic bond A disaccharide is a monosaccharide bonded by a glycosidic linkage creating a bond of 2-di A polysaccharide is a long chain of 3 or more monosaccharides bonded by a glycosidic bond A glycosidic bond is either- Alpha, easy for animals to break, enzymes can break Beta, animals do not make the enzymes to break, dietary fiber 7. Describe the function and structure of starch, glycogen, cellulose, and chitin Starch - polymer of glucose, alpha glycosidic bonds, plant energy storage Glycogen - polymer of glucose, alpha glycosidic bonds, animal energy storage Cellulose - polymer of glucose, beta glycosidic, plant structural molecule Chitin - polymer of modified glucose, beta glycosidic, animal structural molecule 8. Describe the characteristics of a lipid Hydrophobic, do not form polymers, non polar bonds (no charge), store energy 9. Contrast a saturated and unsaturated fatty acid Saturated fatty acids- have all single bonds between carbons, solid at room temp. Unsaturated fatty acids- has one or more double bonds between carbons, forms kinks in chais, liquid at room temp. 10. Describe the structure and function of a triglyceride Energy storage for long term. Glycerol molecule, carb with 3 carbons and 3 fatty acid chains 11. Describe the structure and function of a phospholipid Glycerol, 2 fatty acid chains, phosphate group, and another negative group. Hydrophilic head and 2 Hydrophobic tails 12. Recognize the structure of a steroid and what their functions are To signal molecules, structure is 4 carbon rings 13. Describe the monomer, polymer, and bond of proteins Monomer- amino acids, each has a different R group Polymer- polypeptide (chain) Peptide Bond- between amino acids, ends are different- carboxyl and amino end to the chain Fold-Structure (confirmation)-function 14. Define polypeptide Chain of amino acids 15. Describe why it is important to know if the amino acid side chains are nonpolar, polar, or charged The characteristics of the side chain determine the folding of the protein, which in turn determines the function of the protein 16. Describe the primary, secondary, tertiary, and quaternary levels of protein folding Primary- the exact sequence of amino acids, which amino acids determines overall structure, covalent peptide bonds Secondary- local folds in the polypeptide, alpha helixes and beta pleated sheets, hydrogen bonds Tertiary- 3-D fold of one polypeptide, ionic and hydrogen bonds, with hydrophobic interactions, rarely covalent bonds Quaternary- more than one folded polypeptide (subunits), comes together to form protein 17. Describe what happens when a protein is denatured and what that does to its function When a protein is denatured it ultimately means you are looking at the sequence of the primary structure unfolded, and this gives the protein no function unless it was to fold again 18. Describe the monomer, polymer, and bond of nucleic acids Monomer- nucleotides, phosphate group, negative charge Polymer- DNA and RNA Bond- phosphodiester bond between nucleotides, with different ends 5’ and 3’ antiparallel 19. Describe the function of DNA and RNA Simply genetic information to code 20. Name the differences between RNA and DNA DNA- double stranded, long chain, ATCG sequence RNA- single stranded, shorter chain, AUCG 21. Describe the structure of DNA including: sugar- phosphate backbone, double helix, antiparallel, and complementary base pairing A – T as G – C 5-3 then 3-5 22. Describe the basic structure of a prokaryotic cell Nucleoid- region where DNA is found Ribosome, cytoplasm, singular circular ribosome, with a cell wall- thick structure outside of plasma membrane 23. Describe the structure and function of the organelles and structures of a eukaryotic cell including: the plasma membrane, nucleus, nucleolus, ribosomes, rough and smooth ER, Golgi apparatus, lysosomes, mitochondria, chloroplasts Plasma (cell) Membrane- the semipermeable membrane surrounding the cytoplasm of a cell Nucleus- area that contains the DNA Nucleolus- dark staining spot inside the nucleus, where RNA is found Ribosomes- RNA and protein particles that make protein, Free- make proteins for inside the cell, Bound- make proteins to export out of call, located on the rER Rough and Smooth ER- Rough, covered in ribosomes- proteins are made to export, Smooth, no ribosomes- lipid synthesis, detox, and store calcium Golgi Apparatus- modify and sort proteins- series of membrane sacks (cisternae), Cist-Entrance-closest to rough ER, Trans-Exit-closest to plasma membrane Lysosomes- Vesicle that has low PH and enzymes to break down macromolecules Mitochondria (powerhouse)- cellular respiration- making ATP using O2, outer and inner membrane, inner cristae and inside is called the matrix, in the folds- contains a “chromosome and ribosomes” Chloroplasts- Photosynthesis, plastids- only in plants. Outer and inner membrane, thylakoid becomes grana- more folds=more photosynthesis. Stroma- chromosome and ribosomes found here 24. Contrast free and bound ribosomes Free ribosomes are inside the cell floating around, they make protein for inside the cell Bound ribosomes are in the rER and make proteins for export outside of the cell 25. Describe the structure of mitochondria An outer and inner membrane, cristae, and matrix 26. Describe the structure of chloroplasts Outer and inner membrane with the stroma in the inner membrane, grana which makes stacks to become the thylakoid, stroma which chromosomes and ribosomes are found in 27. Name the three types of cytoskeleton Thickest- Microtubules Intermediate Filaments- anchors to pull chromosomes Microfilament- skinniest 28. Describe the cell wall and name the types of cells that have one Cell wall is an extracellular structure outside of the cell membrane. Plant, Fungi, and Prokaryotes have cell walls 29. Describe the extracellular matrix Proteins and other small molecules outside of the cell 30. Describe what is meant by a selectively permeable membrane Some things can pass through, including hydrophobic organelles 31. Define peripheral and integral membrane proteins Peripheral- proteins on outside edges of the membrane, stick to membrane because they interact with other organelles in the membrane, are not hydrophobic Integral- proteins that go deep into the membrane, has a hydrophobic part on the protein 32. Describe the process of diffusion Movement of molecules from a HIGH concentration to a LOW, perfume in a room in order to move down the concentration gradient 33. Describe the process of osmosis Movement of water through a semi-permeable membrane from an area of LOW SOLIUTE concentration to an area of HIGH SOLUTE concentration, water can cross but solute cannot 34. Define isotonic, hypertonic, and hypotonic Hypertonic- more solute, water will move out of the cell to the more concentrated solute areas Hypotonic- less solute, meaning more water will want to move into the cell Isotonic- same concentration, balanced movement into and out of the cell 35. Define facilitated transport Proteins help molecules cross across the semipermeable membrane 36. Compare and contrast channel proteins and carrier proteins Channel proteins- make tube through the membrane, small molecules, aquaporin’s, H2O Carrier proteins- bind and then transport, larger molecules, really specific movement 37. Compare and contrast passive and active transport Passive- things that can move through the membrane and phospholipid bilayer, small and hydrophobic molecules move through, large and hydrophilic charged molecules cannot move through- proteins needed to help Active- move molecules AGAINST diffusion to an area of high concentration- requires energy “ATP” 38. Describe the process of exocytosis and endocytosis Exocytosis- inside, using a vesicle to bring something into the cell Exocytosis- outside, using a vesicle to release something out of the cell EX. Golgi A.


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