Exam 1 study guide
Exam 1 study guide biology 1305
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This 15 page Study Guide was uploaded by star ornelas on Friday September 11, 2015. The Study Guide belongs to biology 1305 at University of Texas at El Paso taught by Horacio O. Gonzalez in Fall 2015. Since its upload, it has received 1210 views. For similar materials see General Biology in Biological Sciences at University of Texas at El Paso.
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Date Created: 09/11/15
Biology 1305 Practice Test 1 W Link to which has the answers httpsquizletcom36068805biologypracticetest1 ashcards 1 2 3 4 5 Define the neutron b A subatomic particle with a positive charge 0 A subatomic particle with negative charge d A particle that creates ions in solution C The particle that identifies the atom Define the proton a A subatomic particle with neutral charge 0 A subatomic particle with negative charge d A particle that creates ions in solution C The particle that orbits the nucleus Define the electron a A subatomic particle with neutral charge b A subatomic particle with a positive charge d A particle that creates ions in solution C The particle that identifies the atom What is the atomic number a The number of neutrons identifies the atom b The number of electrons identifies the atom d The number of protons and electrons in an atom 6 None of the above What is a molecule a The electron shells in a compound b A pure substance that contains only one kind of atom c The fundamental unit in chemistry d An atom with low molecular weight 6 7 8 9 The attractive force that links two atoms together is called a Gravitational bond b Electrical bond d Electron shells e Atomic reactivity Define an ionic bond a Sharing of H atom b Interaction of a polar compound with a nonpolar compound d Weak interactions between nonpolar substances e Sharing of electron pairs Define a covalent bond a Sharing of H atom b Interaction of a polar compound with a nonpolar compound c Attraction of opposite charged ions d Weak interactions between nonpolar substances What is a hydrogen bond b Interaction of a polar compound with a nonpolar compound c Attraction of opposite charged ions d Weak interactions between nonpolar substances e Sharing of electron pairs 10 What are Van der Waals forces 11 The attractive force that an atomic nucleus exerts on electrons is called a Sharing of H atom c Attraction of opposite charged ions d Weak interactions between nonpolar substances e Sharing of electron pairs a Electricity 12 Is Oxygen and electronegative element c Ionic force d Polarity e Relativity b No c Oxygen is electropositive d Only in water e None of the above 13 Which of the following is the correct order in decreasing order for the relative strengths of chemical bonds Assume physiological conditions b Van der Waals forces covalent hydrogen ionic hydrophobic interactions c van der Waals forces hydrophobic interactions covalent ionic hydrogen d Hydrogen covalent van der Waals forces ionic hydrophobic interactions e Hydrophobic interactions ionic van der Waals forces hydrogen covalent 14 The building blocks of sugars are a Aminoacids b Nucleotides c Simple lipids d Oligosaccharides 15 The following is a disaccharide b Ribose c Deoxyribose d Starch e Glucose 16 The main function of oligosaccharides is to a They act as an external plant support c They degrade toxic cellular metabolites d The induce cellular death e Their function is unknown to science 17 The following are examples of polysaccharides a Cellulose W b Starch c Glycogen e None of the above 18 What characteristic of ribose makes RNA less stable than DNA a The fact that ribose is a pentose with five carbon atoms c The fact that uracil is present in RNA and not in DNA d The fact that ribose creates a very long RNA molecule e The presence of a mutation in ribose 19 What is the difference between ribose and deoxyribose b Ribose is a pentose deoxyribose is a hexose c Ribose is a component of nucleic acids deoxyribose is a component of proteins d Ribose is a monosaccharide deoxyribose is a polysaccharide e Their differences are negligible there is no functional difference between them 20 Lipids are not strictly considered biopolymers because a There is no single monomer to synthesize lipids b Lipids are composed of aminoacids and sugars d Lipids are polar e Lipids are hydrophilic 21 What is the difference between saturated and unsaturated fatty acid 0quot v Saturated fatty acids are very long unsaturated fatty acids are very short c Saturated fatty acids contain carbon atoms unsaturated fatty acids contain sulfur atoms Saturated fatty acids are polar unsaturated fatty acids are non polar e Saturated fatty acids are present only in plants unsaturated fatty acids are present only in animals 0 v 22 Why should we limit our dietary intake of saturated fatty acids a Saturated fatty acids provide a lot of energy b Diabetes has been linked to diets With high contents of saturated fatty acids c Saturated fatty acids are mutagenic d Saturated fatty acids have a high melting point they can burn our body 23 What are the components of a nucleotide b A nucleic acid sugar and a nitrogen containing base c A nitrogen containing base and a phosphate group d The purines and pyridimines e None of the above 24 What are the names of the purines and their main structural feature a Adenine and thymine they form complementary bonds in DNA b Guanine and cytosine they are prone to mutation d Uracil and thymine both are components of DNA e Cytosine Thymine and Uracil they are single ring bases 25 What are the names of pyridimines and their main structural feature a Adenine and thymine they form complementary bonds in DNA b Guanine and cytosine they are prone to mutation c Adenine and guanine they are double ring bases d Uracil and thymine both are components of DNA 26 The 5 to 3 directionality means a The direction in Which proteins grow c The direction of polysaccharide synthesis d The plane in Which cells are diVided e The orientation of phospholipids Within cellular membranes 27 What is transcription a The process of DNA replication c The synthesis of proteins using an RNA template d The synthesis of noncoding DNA in cells e None of the above Q 28 What is translation a The process of DNA replication b The synthesis of RNA using DNA as template d The synthesis of noncoding DNA in cells e None of the above 29 Describe the components of an aminoacid b Carbon hydrogen and oxygen CH and O 0 Three fatty acids and a glycerol molecule d A phosphate group a sugar and a nitrogen base e None of the above 30 What defines a protein primary structure 0quot v Repeated spatial uhelix and Bpleated sheet patterns in polypeptide chains 0 The polypeptide chain is bent at specific sites and then folded back Two or more polypeptide chains called subunits are connected and fold to create this level of structure There is no primary structure in proteins 0 v 39D 31 What defines a protein secondary structure a The precise sequence of aminoacids in a polypeptide c The polypeptide chain is bent at specific sites and then folded back d Two or more polypeptide chains called subunits are connected and fold to create this level of structure e There is no secondary structure in proteins 32 What defines a protein tertiary structure a The precise sequence of aminoacids in a polypeptide b Repeated spatial uhelix and Bpleated sheet patterns in polypeptide chains d Two or more polypeptide chains called subunits are connected and fold to create this level of structure e There is no tertiary structure in proteins 33 What defines a protein quaternary structure a The precise sequence of aminoacids in a polypeptide b Repeated spatial uhelix and Bpleated sheet patterns in polypeptide chains c The polypeptide chain is bent at specific sites and then folded back e There is no quaternary structure in proteins 34 Abnormal elevated temperatures may degrade proteins Possible reasons for this is are b Proteins may abnormally react With compound in cells under heat stress c Elevated temperatures increase reaction rates d High temperature increase the concentration of nonpolar substances e The proteins are not transcribed under elevated temperatures 35 The name of the reactant in an enzyme catalyzed reaction is called a Prosthetic group b Cofactor c Coenzyme d Active site 36 The site of the enzyme Where catalysis takes place is the a Prosthetic group b Cofactor c Coenzyme e Substrate 37 An inorganic ions that binds certain enzymes is a a Prosthetic group c Coenzyme d Active site e Substrate 38 A carboncontaining molecule required for the action of enzymes is a a Prosthetic group b Cofactor d Active site e Substrate 39 A nonaminoacid group that is attached permanently to enzymes is called b Cofactor c Coenzyme d Active site e Substrate 40 The change in shape of an enzyme due to regulation is defined as b ActiVism c Cooperation d Condensation e Hydrolysis Biology 1305 1St TEST CONCEPTS KNOW THE DEFINITIONS AND CONCEPTS FOR THE FOLLOWING 1 Atom The smallest unit of matter Consists of nucleus and one or more electrons Neutron A subatomic particle with neutral charge ProtonA subatomic particle with positive charge Electron A subatomic particle with a negative charge Atomic numberThe number of protons in the nucleus of an atom Molecule Chemical substance made up of two or more atoms joined by covalent bonds or ionic attractions Octet rule Process in which atoms undergo whereby they obtain give up or share electrons so that their outer valence shell contains eight electrons Chemical bond An attractive force stably linking two atoms Ionic bond An electrostatic attraction between positively and negatively ions 10 Covalent bond chemical bond that involves the sharing of electron pairs between atoms 11 12 13 14 15 16 17 18 19 20 21 Polar bond covalent bonding is a type of chemicalbond where a pair of electrons is unequally shared between two atoms Nonpolar bond chemical bond where two atoms share a pair of electrons with each other Hydrogen bond the electrostatic attraction between polar molecules Van der Waals forces sum of the attractive or repulsive forces between molecules Properties of water chemical substance with chemical formula H 20 one molecule of water has two hydrogen atoms covalently bonded to a single oxygen atom Functional groups An atom or group of atoms that replaces hydrogen in an organic compound Functional groups define the structure of a family of compounds and determine its properties Hydroxyl group carbon of a carbonyl group CO produces a carboxyl group COOH that is the defining group of a carboxylic acid Aldehyde group a carbonyl center a carbon double bonded to oxygen bonded to hydrogen and an R group Keto group is an organic compound with the structure RCOR Carboxyl group weak acids dissociating partially to release hydrogen ions Phosphate group as an inorganic chemical is a salt of phosphoric acid 22 Amino group functional group that consists of a nitrogen atom attached by single bonds to hydrogen atoms alkyl groups aryl groups or a combination of these three 23 Sul aydryl group functional group consisting of a sulfur bonded to a hydrogen atom 24 Carbohydrates biological molecule consisting of carbon C hydrogen H and oxygen 0 atoms 25 Monosaccharideshe building blocks of disaccharides such as sucrose and lactose and polysaccharides such as cellulose and starch 26 Disaccharidesa sugar a carbohydrate composed of two monosaccharides 27 Oligosaccharides a saccharide polymer containing a small number typically three to nine of simple sugars monosaccharides 28 Polysaccharidespolymeric carbohydrate molecule composed of long chains of monosaccharide units Glycogen cellulose and starch 29 RiboseRibose is an organic compound With the formula C 5H100 5 speci cally a pentose monosaccharide with linear form H CHOH4 H Which has all the hydroxyl groups on the same side in the Fischer projection 30 DeoxyriboseDeoxyribose or more precisely 2deoxyribose is a monosaccharide With idealized formula H CHOH3 H Its name indicates that it is a deoxy sugar meaning that it is derived from the sugar ribose by loss of an oxygen atom 31 32 33 34 35 36 37 38 39 40 GlycogenGlycogen is a multibranched polysaccharide of glucose that serves as a form of energy storage in animals and fungi StarchStarch or amylum is a carbohydrate consisting of a large number of glucose units joined by glycosidic bonds Cellulose a long chain made by the linking of smaller molecules The links in the cellulose chain are a type of sugar BDglucose main component of the plant cell wall Pentosea monosaccharide With five carbon atoms Hexose a monosaccharide With six carbon atoms haVing the chemical formula C6H1206 Glycosidic bond covalent bond that joins a carbohydrate sugar molecule to another group which may or may not be another carbohydrate Lipid a group of naturally occurring molecules that include fats waxes sterols fat soluble Vitamins monoglycerides diglycerides triglycerides phospholipids and others Saturated fatty acid In saturated fatty acids all the bonds in the carbon atoms are single Unsaturated fatty acid unsaturated fatty acids contain one or more double bonds Metabolism chemical transformations Within the cells of liVing organisms 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 Anabolic reaction refers to chemical reactions in which simpler substances are combined to form more complex molecules Catabolic reaction usually release energy that is used to drive chemical reactions Energy The ability to do work or produce change Nucleic acids include DNA deoxyribonucleic acid and RNA ribonucleicacid are made from monomers known as nucleotides Nucleoside is a nucleobase linked to a sugar Nucleotide A nucleic acid sugar a nitrogen containing base and a phosphate group PurinesAdenine and guanine they are double ring bases PyridimiesCytosine Thymine and Uracil they are single ring bases 5 to 3 direction The direction in which DNA and RNA grow TranscriptionThe synthesis of RNA using DNA as template TranslationThe synthesis of proteins using an RNA template Protein Proteins are large biomolecules or macromolecules consisting of one or more long chains of amino acid residues Functions of protein They do most of the work in cells and are required for the structurefunction and regulation of the body39s tissues and organs Aminoacids organic compounds composed of amine and carboxylic acid functional groups along with a sidechain specific to each amino acid Classification of aminoacids An alpha carbon a carboxyl and an amino group a hydrogen atom and a radical R group 56 Primary structure of a proteinThe precise sequence of aminoacids in a polypeptide 57 Secondary structureRepeated spatial uhelix and Bpleated sheet patterns in polypeptide chains 58 uhelix Left handed direction the second form of regular secondary structure in proteins 59 Bpleated sheet Right handed direction the second form of regular secondary structure in proteins 60 Tertiary structure of a proteinRepeated spatial uhelix and Bpleated sheet patterns in polypeptide chains 61 Quaternary structure of a proteinTwo or more polypeptide chains called subunits are connected and fold to create this level of structure 62 Protein denaturation the disruption and possible destruction of both the secondary and tertiary structures 63 Enzymes are biological molecules proteins that act as catalysts and help complex reactions occur everywhere in life 64 Substrate is a molecule upon Which an enzyme acts 65 Enzyme mode of action 66 Cofactor is a nonprotein chemical compound that is required for the protein39s biological actiVity 67 Coenzyme a nonprotein compound that is necessary for the functioning of an enzyme 68 Prosthetic group bound tightly to proteins and may even be attached through a covalent bond as opposed to coenzymes Which are loosely bound may be organic such as a vitamin sugar or lipid or inorganic such as a metal ion but is not composed of amino acids 69 Allosterism A change in the activity and conformation of an enzyme resulting from the binding of a compound at a site on the enzyme other than the active binding site
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