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BIOL 190

by: Stacy Downing

BIOL 190 BIOL 190

Stacy Downing
GPA 3.94

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Studying this really helps you with the exam
Introductory Biology for health professions
preeti shah
Study Guide
50 ?




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This 3 page Study Guide was uploaded by Stacy Downing on Saturday January 30, 2016. The Study Guide belongs to BIOL 190 at Towson University taught by preeti shah in Spring 2016. Since its upload, it has received 28 views. For similar materials see Introductory Biology for health professions in Biology at Towson University.


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Date Created: 01/30/16
Unit 2 Review- Biological Molecules Categorizing Proteins  Structural  Globular or Fibrous  Functional o Transport: movement of material in/out of cell (Hemoglobin carries O2 around body) o Hormone: chemical signaling in the body (insulin/glucagon regulates blood sugar levels) o Contractile: contraction (myosin which are muscle contractions) o Structural: structural support, toughness (collagen in the EMG holds the body together) o Protection: (antibodies creates immunity in white blood cells) o Enzyme: needed to facilitate reaction in body (amylase digest starch in saliva) o Storage: nutrient storage for growing embryo (endosperm in seeds) Amino Acids  There are 20 amino acids  Amino group, central carbon, hydrogen atom, carboxyl group, R group (side chain- different for each amino acid)  R group vary in… o Size o Charge (+ or – or neutral) o Polarity  Small R groups allow bending of the chain, Large prevent bending  Water Solubility o Hydrophilic (charged and polar R groups) water soluble o Hydrophobic (uncharged and nonpolar R groups) not water soluble Dehydration Synthesis  Formation of a covalent (peptide) bond between 2 amino acids to form a chain (polypeptide)  Releasing a water molecule  The covalent bond between 2 amino acids = peptide bond Polypeptide  A chain of amino acids by dehydration synthesis through covalent bonds( NOT FUNCTIONAL)  1° structure: the specific sequence of amino acids  2° structure: the alpha helices and beta sheets, weak hydrogen bonds  3° structure: folds the alpha helices and beta sheets creating the 3D overall structure of the protein using ionic bonds, hydrogen bonds, disulfide bonds, hydrophobic interaction between R groups to maintain stability  4° Structure: a functional protein consisting of more than 1 polypeptide chain Protein Examples  Glucagon: raises blood glucose level, functional at 2° structure  Amylase: hydrolyzes starch in the salvia, functional at 3° structure  Hexokinase: catalyzes first reaction in glycolysis, functional at 3° structure  Hemoglobin: carries oxygen throughout the body, functional at 4° structure  K+ Channel: membrane transport protein, functional at 4° structure  Collagen: holds ligaments together, functional at 3° structure Dehydration Synthesis Denaturation: loss of 4° 3° 2° o Rise of heat, raise or loss of pH or salt Hydrolysis: loss of 1° structure o Enzyme required Gene Mutation  Permanent change to the DNA sequence  2 Main classes of Gene Mutation o Base Substitution (Point Mutation)  Silence: no change in protein  Nonsense: premature stop  Missense: amino acid substitution  Example: sickle cell anemia (TA to AT, Glu to Val, sickled hemoglobin and RBC’s, stuck in capillaries ad cause pain crisis-> destroyed by spleen) o Base insertion/deletion  Frameshift: Reading-frame of codons is shifted by 1 or 2 amino acids  Amino acid insertion: extra codon inserted, but same reading frame Protein structure/function relationship  Alter 3D structure, alter the function  Denaturation, Mutation, Hydrolysis 4 Main Classes of Biomolecule  Nucleic Acid: DNA Biomolecule Polymer Monomer and RNA (mRNA, tRNA, rRNA) Protein Protein Amino Acid  Protein Carbohydrates Polysaccride Monosaccri de  Carbohydrates: Nucleic Acid DNA RNA Nucleotides mono-, di-, poly- saccrides Lipids TriglyceridesGlycerol o Atoms: CHO, ratio 1C:2H:1O o Maltose= and Fatty glucose + glucose Acids o Sucrose= glucose + fructose o Lactose = glucose + galactose o Cellulose= Dietary Fiber, cannot digest, function as structure in plants o Starch: long term storage in plants o Glycogen: long term storage in animals  Lipids: triglycerides, phospholipids, steroid, waxes o Atoms: CH (a little O) o Hydrophobic o Triglycerides contain 3 fatty acids and 1 glycerol, long term energy storage o Phospholipid contain 2 fatty acids, PO4group, 1 glycerol, membrane structure o Cholesterol = Steroid, hormones and membrane structure o Waxes: protection o Fatty Acid: saturated(unhealthy), unsaturated (healthier) cis, trans ATP  Specialized nucleotide  Adenine base, ribose sugar, 3 PO4 groups  Immediate energy molecule What do all 4 classes have in common?  Organic contains at least 1 carbon and covalently linked hydrogen  Contains one or more chemical groups  Fabrication from monomers: dehydration synthesis  Degradation to monomer: hydrolysis 2 Kinds of covalent bonds  Nonpolar o Partner atom share e equally o Partner atoms are neutral o Examples: H-H bond, C-H bond o HYDROPHOBIC o Methane is nonpolar  Polar o Partner atom share e unequally o Partner atoms have opposite partial charges o HYDROPHILLIC o Water and glucose is polar o Charged particles are also water soluble Chemical groups  Hydroxyl group: polar, found in sugars, CHO’s, glycerol  Carbonyl group  Carboxyl group: acid, negatively charged, found in amino acids, protein, fatty acids  Amino group: base, positive charged, found in amino acids, protein, phospholipid head  Phosphate group: buffer, negatively charged, found in nucleic acids, ATP, phospholipid head  Methyl group: nonpolar, found in fatty acid, lipids Atoms present in Biomolecule  Proteins: C H O N a little S  Carbohydrates: C H O 1C:2H:1O  Lipids: C H a little O  Nucleic acid: C H N O P


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