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Intro to Biology week 3

by: emmy_rose4267

Intro to Biology week 3 BIOL 107-06

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These notes cover the lectures for week 3
Introduction to Biology I
Daniela Ostrowski
Class Notes
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This 2 page Class Notes was uploaded by emmy_rose4267 on Friday September 9, 2016. The Class Notes belongs to BIOL 107-06 at Truman State University taught by Daniela Ostrowski in Fall 2016. Since its upload, it has received 4 views. For similar materials see Introduction to Biology I in Biology at Truman State University.


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Date Created: 09/09/16
Intro to Biology  9/6  Carbohydrates cont.  3) Polysaccharides: many monosaccharides bonded together  Starch, cellulose, chitin, and glycogen  Starch consists entirely of a alpha glycosidic linkage  Glycogen is stored in liver and muscles  Cellulose: major component of the cell wall in plants, but we lack the enzyme to break it  down  Chitin is found in cell walls of fungi, protists, and exoskeleton of insects and  crustaceans.    Lipids   Lipids:​ carbon­containing compounds that are found in organisms and are largely  nonpolar and hydrophobic.   Saturated: single bonds between carbons  Unsaturated: double bonds between one or more pairs of carbon atoms  ­Fluidity depends on length and saturation of their hydrocarbon  1) Fat: composed of 3 fatty acids that are linked to a 3 carbon molecule called  glycerol  Trans fats raise bad cholesterol levels and lower your good levels  2) Phospholipids: glycerol that is linked to a phosphate group and 2 hydrocarbon chains   Amphipathic: substances that contain both hydrophilic and hydrophobic regions  3) Steroids: lipids in which carbon skeleton contains 4 fused rings  ­Different steroids vary in chemical groups attached to the rings  Anabolic Steroids: synthetic variation of the male hormone testosterone    Proteins  1) Enzymes: catalyze chemical reactions  2)Transport proteins: regulate molecules to enter or exit cells  3)Defensive proteins: attack and destroy viruses or bacteria  4)Receptor proteins: carry and receive signals from cell to cell  5) Structural proteins: motor proteins and contractile elements that help with movement  6) Storage: proteins are made of amino acids that help with embryo development  Monomer: amino acids  In solution: amino group attracts protons and carbonyl group loses protons  R­group: 20 different bonds that are either polar or nonpolar  Essential amino acids: can not be produced by your body (mainly animal origin)  Condensation (dehydration) reaction: links carboxyl group of one amino acid to the  amino group of the next amino acid as water  Hydrolysis: breaks polymer apart by adding water molecule  Peptide bond: bond between the carboxyl group of one amino acid and amino group of  another  Covalent bond: has characteristics of a double bond   ­Protein vary in size, shape, and chemical properties  1)Primary structure: sequence of amino acids in polypeptide chain  2) Secondary structure: shape of amino acid chains (due to H bonding)  3) Tertiary structure: 3D shape due to bonding between the secondary structures  4) Quaternary Structure: arrangement of polypeptide chains if there are 2 or more  chains  ­Protein folding is more stable than unfolded molecules      How proteins bond together  1) Hydrogen bonds  2) Hydrophobic interactions  3) Van der Waals interactions  4) Covalent bonds  5) Ionic bonds    9/8  REVIEW DAY, NO NOTES!    Exam on Tuesday           


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