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Biology 101 Notes

by: Franchesca Runde

Biology 101 Notes Biology 101

Franchesca Runde

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These notes cover the first lecture up to types of transport for membrane proteins. This material will be covered in exam 1.
Animal Biology
Sharon L Thoma, Kurt J Amaan
75 ?




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This 8 page Bundle was uploaded by Franchesca Runde on Saturday February 13, 2016. The Bundle belongs to Biology 101 at University of Wisconsin - Madison taught by Sharon L Thoma, Kurt J Amaan in Summer 2015. Since its upload, it has received 55 views. For similar materials see Animal Biology in Biology at University of Wisconsin - Madison.


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Date Created: 02/13/16
Biology 101 Prokaryotes- no nucleus (bacteria and archaea) Eukaryotes- do have nucleus (protists, animals, plants, fungi) Animals  Eukaryotic  Multicellular  Heterotrophic (ingest food)  Lack cell wall  Bodies made up of cells organized into tissues  Motile  Specific development patterns Proteins Single unit protein – monomer (amino acid) If there’s a + or – in the R group, the amino acid is charged, which means it’s water soluble OH SH polar covalent bonds that act like they’re charged (water soluble) NH Hydrophilic – water hating Hydrophobic – water loving Two amino acids – dipeptide Many amino acids – polypeptide There can be many different forms of polysaccharides because they can be a combination of any of the multiple amino acids Each saccharide has an amino group and a carboxyl group There are four levels of protein structure 1. Primary – linked series of unique sequence amino acids; always starts with amino group and ends with carboxyl group; 20^n possible combinations 2. Secondary – localized folding patterns created by hydrogen bonding; interactions between non R-groups; Alpha-helix (phone cord) and Beta pleated sheet shape; keratin is done after this step 3. Tertiary – overall 3-dimensional shape; interactions between R-groups; globular proteins a. Hydrogen Bonds – H atom experiences attraction to an electronegative atom b. Disulfide Bonds – formed between two sulfur atoms (covalent) c. Ionic Bonds – attractions between + and – d. Hydrophobic Exclusion – hydrophobic amino acids go towards the interior while the hydrophilic go towards the exterior (Chaperone proteins help proteins fold into their correct tertiary structure) 4. Quaternary – aggregation of 2 or more polypeptides A change in primary structure won’t necessarily affect other structures and functions, but it could Enzymes Biological catalysts Speeds up rates of chemical reactions so we can use it Active site – pockets in enzymes that allow only one substrate to fit Induced fit – enzyme substrate complex The physical condition a protein is in affects folding Denaturing – unfolding, happens if you move away from optimal conditions If it unfolds only slightly, sometimes the chaperone protein can save it Optimal temperature for human enzymes is 96 degrees Things slow down as temperature gets colder If temperature gets too hot, enzymes can be destroyed pH balance – low number = acidic, high number = alkaline High concentration of H+ = acidic, high OH concentration = basic pH for pepsin (found in the stomach) = 2, pH for trypsin (found in small intestine) = 8 Lipids Hydrophobic molecules Functions: Hormones, energy storage, major component of cell membranes 1. Sterols (steroids) have many functions; 4-ring structure a. Hormones (estrogen, testosterone, cortisol) b. Membrane Structure (cholesterol) Cholesterol moves in blood as part of a lipoprotein complex Apolipoproteins – proteins found in lipoprotein complexes c. Low Density Lipoprotein (LDL) – carries cholesterol from liver to cells (L for Lowsy) d. High Density Lipoprotein (HDL) – picks up excess cholesterol from cells and delivers to the liver for disposal/recycling (cleans up after LDL) 2. Fats and Oils (Triglycerides) a. 3 fatty acids b. Fats and oils found in plants and animals c. Function – high energy storage (covalent bonds = energy) d. Many C-H bonds make it hydrophobic e. Can be any length f. Can have different degrees of saturation Saturated bonds are all single, so they’re straight Unsaturated fats have double bonds which causes a bend Saturated fats pack tightly together, unsaturated fats are more loosely packed Animal fat – saturated fat Solid and room temperature (hamburger meat) Plant fat – unsaturated fat Liquid at room temperature (canola oil) Unsaturated fats are healthier High saturated fat diet – increased levels of LDL and HDL in blood stream, negative effects High unsaturated fat diet – decrease In LDL ad increase in HDL, positive effects Trans fats are liquid at room temperature and unsaturated 3. Phospholipids (components of cell membrane) a. Only two fatty acids b. Phosphate - containing head group: negative charged, water soluble, hydrophilic c. Fatty acids – “bottom legs” hydrophobic d. Amphipathic – both hydrophilic and hydrophobic In water, what will phospholipids do? Micelles form – hydrophilic heads go on the outside, hydrophilic tails go towards the inside (like Lipoprotein, hydrophobic parts would touch cholesterol) Bilayers can form – hydrophilic touches water, hydrophobic stays inside Proteins are transmembrane if they go all the way through Peripheral membrane proteins don’t reach the bilayer Oligosaccharide (hexagonal carbohydrate) is attached to proteins on the top A protein with an oligosaccharide attached is called a glycoprotein Glycoproteins tell the body which type of cell for which organ – Cellular ID tags Cholesterol OH polar covalent bond interacts with head, the rest interacts with the tail, stabilizes membrane structure Cytoskeleton – peripheral membrane protein Fluid Mosaic model of a membrane structure Fluid – phospholipids and proteins can move around Mosaic – has proteins throughout Membranes are fluid Most proteins can move, all phospholipids can Phospholipids move laterally through the bilayer Fluidity depends on:  Temperature o At body temperature the bilayer is fluid o Lower temp = slower movement o Freezing temp = membrane solidifies and is no longer permeable o High temp = melting  Lipid Composition o Saturation of hydrocarbon fatty tail – unsaturated = more fluid, saturated = less fluid o Increased permeability as fluidity increases o Unsaturated stays fluid at lower temps o Saturated freezes faster  Length of fatty acids (hydrocarbon tails) o Longer tail = less fluid = stronger hydrophobic reaction  Cholesterol o At high temps – reduces membrane fluidity (compared to less or no cholesterol) o At low temps – helps membrane stay fluid with more cholesterol o More cholesterol inhibits packing of phospholipids Membrane Remodeling Prokaryotes Plants Cold-Blooded animals Enzyme Desaturase – inserts double bond into fatty acid making the membrane more fluid = lower freezing temp What do membrane proteins do? Enzymes Cell to cell recognition Attachment Cell joining Signaling Transport  Passive o Simple diffusion – doesn’t require energy, moves from high to low concentration (down the gradient), No proteins needed, no ATP o Small uncharged, hydrophobic molecules can pass through, gases can move through, water can move through at a very slow pace (pores open up in membranes) o Large polar molecules and ions can’t move through o Facilitated Diffusion – movement down the gradient, no energy investment, but (transmembrane) proteins are needed o Channel proteins – pore forming proteins, transmembrane (like sticking a straw through) o Many channel proteins are gated – open/close in response to stimulus or chemical signal o Selective permeability – only allow specific substances through o Rapid response – chemical can flood in and out o Carrier protein – change shape upon binding to the substance they transport o Glucose binds, changes proteins’ shape, it releases glucose, then returns to its original shape = slower response o Osmosis – passive transport of water only o moves down the concentration gradient, no energy or proteins needed unless massive water movement is required Hypertonic – amount of something dissolved in water (more than hypotonic, less water) Hypotonic – less substance dissolved, more water Water always moves from hypo to hyper Osmosis is a combination of simple and facilitated diffusion Aquaporins – water channel proteins They are the circle that water enters through - hydrophilic ring Hydrophobic exterior latches it onto the protein Water moves into cells with AQP faster  Active Transport o Moving substance against the concentration gradient o Low concentration High concentration o Energy investment required (ATP) o Adenosine Triphosphate o High energy phosphate bonds o Proteins required (active transport proteins) Pumps – Sodium/Potassium pump Sodium out, potassium in Phosphate added by ATP, proteins turned upside down Bulk Transport (vesicular) Movement of substances into and out of the cell by vesicles Vesicle – membrane bound sac found inside a cell Exocytosis – substance released from cell through vesicle, fuses with plasma membrane, opens up and releases substance Endocytosis – plasma membrane vaginates and brings in substance


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