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● Anatomy : study of bodily structures ● Physiology : study of body’s processes & functions Right Upper Quandrant (Liver/Gallbladder) Left Upper Quadrant (Stomach/Spleen) Right Lower Quadrant (Small Intestine/Appendix) Left Lower Quadrant (Urinary) 18. Define: Monomer, polymer ● Monomer = atoms or small molecules that bond together to form more complex structures such as polymers; 4 types: sugars, amino acids, fatty acids, and nucleotides . Fa.Aa.N.S ● Polymer = materials made of long, repeating chains of molecules ● List & give examples of the following macromolecules in the body: Macromolecule Examples of polymers in the Body Carbohydrates Sugars, fibers & starches (SFS) Proteins antibodies, contractile proteins, enzymes, hormonal proteins, structural proteins, storage proteins, and transport proteins Nucleotides DNA, RNA, ATP, NADP+ 20. Lipids ● Describe the general structure of: ○ Fatty acids straight chain of an even number of carbon atoms, with hydrogen atoms along the length of the chain and at one end of the chain and a carboxyl group (―COOH) at the other end; 3 types: ○ Glycerides esters formed from glycerol reacting with fatty acids, generally hydrophobic

○ Steroids lipid compound composed of four hydrocarbon rings bonded to a variety of other atoms and molecules ○ Phospholipids hydrophobic tails, containing the neutral fatty acids which acts as barrier from keeping stuff from freely crossing membrane, and hydrophilic heads, containing the charged phosphate groups and nitrogen atom which face both in and outside cell. ○ Glycolipids composed of a carbohydrate unit linked to a single or multiple fatty acid(s) Phospholipid Similarities Differences Phospholipids - Lipids - Glycerol backbone - Triglycerides are made of 1 glycerol and 3 fatty acid hydrocarbon chains. Phospholipids have a phosphate group and only have 2 fatty acid hydrocarbon chains. - Diff chemical structures Fatty acids Triglycerides Amino Acids & Proteins ● Describe how peptide bonds are formed: a covalent bond between two amino acids that forms by dehydration synthesis. ● Define: ○ Primary: sequence of amino acids of which it is made ○ Secondary: alpha helix; a strand of amino acids that maintain a stable spiral shape with the help of hydrogen bonds, which create bridges between different regions of the same strand ○ Tertiary: folded into 3 dimensional shape; amino acids that had been very distant in the primary chain can be brought quite close via hydrogen bonds or, in proteins containing cysteine, via disulfide bonds. A disulfide bond is a covalent bond between sulfur atoms in a polypeptide. ○ Quaternary structure: Often, two or more separate polypeptides bond to form an even larger protein (ex. Hemoglobin (globular protein) + Collagen (fibrous protein)) ● ID in Openstax Figure 2.13: ○ Enzyme: catalyst composed of protein or ribonucleic acid (RNA),

○ Substrate: reactant in an enzymatic reaction. ○ Reactants: one or more substances that enter into the reaction. ○ Products: one or more substances produced by a chemical reaction Macromolecules Glycoproteins Carbs + large proteins Proteoglycans polypeptides + large polysaccharides Glycolipids carbohydrate chains + lipids ● ID the 3 main parts of a nucleotide: Phosphate, sugar, nitrogen base ● Nucleotide: foundation of the genetic code with the instructions on how to build and maintain the human body from conception through old age. There are about three billion of these base pairs in human DNA. ○ Draw: Carbon, hydrogen, phosphate, nitrogen, oxygen atoms, all bonds ○ 1. Describe types of membrane proteins including:

○ Peripheral membrane proteins attached to the surface of the bimolecular lipid layer ○ Integral membrane proteins embedded in the whole bilayer. Integral proteins have hydrophobic and hydrophilic areas whereas peripheral proteins do not. ○ Glycolipids hydrophobic lipid tail and one or more hydrophilic sugar groups linked by a glycosidic (covalent) bond; structural role to maintain membrane stability but also facilitates cell-cell communication acting as receptors, anchors for proteins and regulators of signal transduction ○ Glycoproteins are large and diverse group of proteins to which one or more sugar molecules, known as oligosaccharides, have been attached through covalent bonding. Attached to polypeptide chains 2. Describe & give general functions of the following: ○ Anchor ○ Receptor protein molecule that contains a binding site for another specific molecule (called a ligand) ○ Channel proteins are membrane-spanning protein that has an inner pore which allows the passage of one or more substances; less selective than carrier proteins, and usually mildly discriminate between their cargo based on size and charge. ○ Carrier proteins are more selective, often only allowing one particular type of molecule to cross. Hypertonic H2O goes out Hypotonic h2O come in Definition Example (from lectures) Symport Also known as cotransport. Two substances move in the same direction at the same time Sodium glucose linked transporter (SGLT) Sodium moves in with glucose in same direction Antiport Also known as countertransport, One substance moves in while another moves out sodium calcium exchanger Facilitated Diffusion High → Low concentration, Glucose moving into

Involves particles that cannot pass through a membrane by themselves. Transport proteins allow movement cell; channel protein exchanges glucose into cell ● Describe the workings of the sodium potassium pump The sodium-potassium pump moves sodium ions out of and potassium ions into the cell. This pump is powered by ATP. For each ATP that is broken down, 3 sodium ions move out and 2 potassium ions move in. ● vesicular transport and categorize them as either importing or exporting things into/from the cell process of a cell exporting material; exocytosis ● Define: ○ Vesicle basic tool used by the cell for organizing cellular substances . Vesicles are involved in metabolism, transport, buoyancy control, and enzyme storage. They can also act as chemical reaction chambers . ○ Endocytosis is the process wherein the materials move into the cell rather than are engulfed by the cell. ■ Endocytosis is usually subdivided into pinocytosis and phagocytosis. ● Pinocytosis endocytosis of fluid ● Phagocytosis endocytosis of large particles ○ Exocytosis is the process of moving materials from within a cell to the exterior of the cell . This process requires energy. 14. Explain the process of DNA replication Initiation, elongation, termination Initiation: two strands are separated ELongation: Each strand becomes a template Termination: completion, original strands bind to new strands ● Describe what RNA polymerase is and its role enzyme that unwinds DNA and then adds new nucleotides to a growing strand of RNA for the transcription phase of protein synthesis 1. List the phases of mitosis in order prophase, prometaphase, metaphase, anaphase and telophase and cytokinesis. (PPMAT+C) 1. Define: ● Regeneration: is the addition of new cells of the same type as the ones that were injured ● Differentiation: unspecialized cells become specialized in structure and function to perform certain tasks in the body.