Zoology 101 Exam 1 - Zoology 101 Exam#1 Study Guide...

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Zoology 101 Exam #1 Study Guide Properties of Life 1. Order/Organization 2. Energy processing a. Sunlight food atp 3. Response to environment a. Sunlight tracks sun 4. Regulation a. Homeostasis (maintain internal conditions despite outside temps) 5. Reproduction 6. Growth and Development 7. Evolutionary adaption (in populations) Molecules Water (H20) -polar molecule -solvent of life -can form hydrogen bond covalent bond -atoms sharing a pair of electrons (charged) -O is more electronegative than H unequal sharing of electrons Polar covalent bond -two ends are different -OH, NH, SH are polar covalent bonds (more electronegative than H) Ions -charged particles -dissolve in water Organic Macromolecules Large molecules, carbon-containing Big molecules are made of small subunits Monomer (1), dimer (2), polomer (multiple) Dehydration reaction -monomer in, water out Hydrolysis -how polymers are broken down -water in, monomer out -Enzymes are needed for building up/breaking down Carbohydrates (sugars) -monomer – monosaccharide -glucose (C6H12O6) -cellular respiration : fuel to make ATP
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-disaccharide -two monosaccharides -sucrose, lactose (broken down by lactase), maltose -quick energy (broken down) Many monosaccharides polysaccharides Starch – storage found in plants Glycogen – storage found in animals -humans can break down starch and glycogen (hydrolytic enzymes) Cellulose –structural found in plants Chitin –structural found in some animals, fungal Proteins Monomer = amino acid -always have amino group, central carbon, carboxyl group, and R group (what changes) Amino Acids -add two together by dehydration =dipeptide (forms peptide bond) -a lot of amino acids hooked = polypeptide Hydrophilic -water loving -form H bonds with H20 -Polar H20 soluble (OH, NH, SH) Hydrophobic -not charged -water hating -do not form H bonds with H20 -not H20 soluble Animals -eukaryotic -multicellular -heterotrophic -ingest food -lack cell wall -bodies made up of cells organized into tissues 4 Levels of Protein Structure 1. Primary a. Structure of amino acids that are in the protein 2. Secondary a. Localized folding created by H bonding
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Interactions between non-R groups b. alpha helix (coils) c. beta pleated sheet (folded) c.i. hydrogen bonds two sheets together (spider web) 3. Tertiary a. Three dimensional shape b. Globular c. Interaction between R group - What interactions between R groups are important in maintaining 3’ structure? 1. hydrogen bonding 2. ionic bonding (+ and – bond) 3. hydrophobic interactions 4. disulfide bridge -hydrophilic amino acids – outside 4.Quaternary (some proteins) a. aggregation of two or more polypeptides b. many polypeptides interact c. Hemoglobin i. 4 polypeptides ii. in red blood cells, bind to oxygen Enzymes -biological catalysts -speed up rate of biochemical reaction -“reusable” -most are protein - Sucrase, hydrolytic enzyme that breaks down the disaccharide sucrose (substrate) into the monosaccharides glucose and fructose (products) -physical conditions affect enzyme function
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Zoology 101 Exam 1 - Zoology 101 Exam#1 Study Guide...

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