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BSC Exam 1 Study Guide

by: Hannah Tomlinson

BSC Exam 1 Study Guide BSC 114

Hannah Tomlinson

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Chapters 1-6
Principles Of Biology I
Kimberly Caldwell
Study Guide
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This 9 page Study Guide was uploaded by Hannah Tomlinson on Saturday September 17, 2016. The Study Guide belongs to BSC 114 at University of Alabama - Tuscaloosa taught by Kimberly Caldwell in Fall 2016. Since its upload, it has received 361 views. For similar materials see Principles Of Biology I in Biology at University of Alabama - Tuscaloosa.


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Date Created: 09/17/16
Biology Exam 1 Chapter 2  Chemical reactions: exchanging and sharing of electrons between atoms  Chemical bonds are formed between atoms  Types of bonds -Covalent -Ionic -Hydrogen Covalent Bonds  Covalent: sharing of a pair of valence electrons between 2 atoms -Electronegativity: attraction of an atom for the electrons of a covalent bond -The more electronegative an atom is, the more strongly it will pull shared electrons toward itself -Nonpolar and polar covalent bonds share electrons differently  Nonpolar Covalent Bonds (atoms are shared): 2 elements end up being equally electronegative in a bond -Carbon and Hydrogen nonpolar covalent (They don’t pull electrons to themselves) (They are neutral)  Polar Covalent Bonds (atoms are shared): one atom is more electronegative than the other -Electrons will not be shared equally -Water has unequal sharing so it causes oxygen to have a partial charge and the hydrogens have a partial positive charge. Ionic Bonds  Ionic (atoms are transferred): actual loss and gain of electrons -Typically between metal and nonmetal -Occurs between molecules with opposite charges -Cation: greater positive charge -Anion: greater negative charge Hydrogen Bonds  Hydrogen: a bond between a covalently bonded hydrogen atom and another atom -Involves 2 different molecules -Weakest bond -Constantly being broken and reformed Chapter 3  Water molecules form hydrogen bonds with one another  Water increases in volume and becomes less dense when frozen because of hydrogen bonding  Water is a great solvent  Solvent: the dissolving agent of a solution  Solution: a liquid that is homogenous mix of 2 or more substances  Solute: substance that is dissolved  Only ionic and polar substances will dissolve readily in water  Hydrophobic: substance that is nonpolar and will not dissolve readily in water (oils and fats)  Hydrophilic: water-loving Chapter 4  Basically everything is carbon-based  Carbon Structure- chains -Forms skeletons of most organic molecules -Varies in length, straight, branched, or arranged in close rings -Some have double bonds  Hydrocarbons: organic molecules made of hydrogen and carbon  Isomers: compounds that have the same molecular formula but different structures and different properties  3 types of isomers -Structural -Enantiomers -Geometric  Structural -Differ in covalent arrangements of atoms -Number of possible isomers increases as carbon skeletons increases in size  Enantiomers (3D) -Mirror images of each other -Cell can distinguish these isomers based on different shapes -Usually one isomer is biologically active and the other is inactive  Geometric -Always involves double bonds -All have the same partnership but different in their spatial arrangements  7 functional groups most important in the chemistry of life -Hydroxyl -Carbonyl -Carboxyl -Amino -Sulfhydryl -Phosphate -Methyl  Hydroxyl group -found in alcohols -Polar covalent bond which helps alcohol dissolve in water -Often ends in –ol -Must have OH  Carbonyl group -Can be found at the end of carbon skeleton or within a skeleton -Double bonded to oxygen and bonded to hydrogen  Carboxyl group -Found in carboxylic acids -Hydrogen in this group can be dissociate, makes molecules a weak acid  Amino group -Can accept H+ -Acts as a base -Can accept H+ and will then be –NH + 3  Sulfhydryl group -Helps stabilize structure of some proteins…… -SH -Often forms disulfide bridges which are really strong covalent bonds - -S-S-  Phosphate group -Can bond to a carbon skeleton by one of its oxygen atoms -Has important role in transfer of cellular energy (ATP)  Methyl group -Not reactive like the others, but is a tag that attaches to a bio molecule -CH 3 -Addition of a methyl group to DNA affects the expression of genes -Arrangement of methyl groups in sex hormones affects their shape and function Chapter 5  Carbohydrates: sugars -Ends in –ose for sugars  3 types of carbohydrates -Monosaccharides -Disaccharides -Polysaccharides  Monosaccharides -Molecular formula is some multiple of CH O2 -Has a –OH group attached to the carbon except one, which is double bonded to an oxygen to form a carbonyl group -Major nutrients for cells  Disaccharides -Double sugar -Consists of 2 monosaccharides joined by a glycosidic linkage (a covalent bond formed between 2 monosaccharides) -Most common is sucrose  Polysaccharides -Polymers of many monosaccharides -Consists of a few hundred to a few thousand monos linked together -2 types: Storage and Structural Lipids  Hydrophobic  Mostly composed of hydrocarbon, but have some polar bonds associated with oxygen  3 families of lipids -Fats -Phospholipids -Steroids Fats -large molecules constructed from 2 kinds of smaller molecules  Glycerol and fatty acids  From dehydration reaction  Glycerol is an alcohol  Fatty acids are hydrocarbons of 16-18 carbons -nonpolar C-H bonds in the tails of fatty acids are the reason fats are hydrophobic -fats separate from water because the water molecule bonds to another and exclude fats (like oil and vinegar, 3 fatty acids join to 1 glycerol) -Saturated fat  NO double bonds between carbon in the tail  Vary in length and in number and location of double bonds but saturated fatty acids don’t have double bonds -Unsaturated fat  Have one or more double bonds in the tail  Saturated and unsaturated fats differ in hydrocarbon tails -Trans fats  What are they? o Partially hydrogenated fats o Less vulnerable to becoming rancid than original oils (going bad) Phospholipids -main component of our cell membrane -structurally related to fats -only has 2 fatty acid chains instead of 3 and has a phosphate group (on 3 glycerol) -PO 4roup is negatively charged -sometimes other small molecules that are charged or polar can be linked to a phosphate group to form a variety of phospholipids -Phospholipids in cells  At the surface of a cell the phospholipids are arranged in double layer (bilayer)  Hydrophilic head: on outside of bilayer  Tails pointed toward interior of membrane, away from water Steroids -carbon skeletons consisting of 4 interconnected rings  Proteins  Account for more than 50% of dry weight of cells  Structurally complex but comprised of amino acids  Consists of -Alpha carbon bonded to a hydrogen -Carboxyl group -Amino group -Side chain symbolized by R  Amino Acids  Processing both carboxyl groups  Identification of Amino Acid Type -Nonpolar R groups will share electrons equally (typically composed of hydrocarbon) -Polar R groups: electrons will not be shared equally (possess functional groups like OH and SH) -Acidic: these R groups contain carboxyl groups (COOH) -Basic: these R groups contain amino groups and have N+  Does not have oxygen associated in the R group  Amino Acids are linked to for protein polymers  Condensation synthesis  The carboxyl group of amino acid is joined to the amino group of another  4 levels of a protein structure -Primary -Secondary -Tertiary -Quaternary Primary  Unique sequence of amino acids of a protein  This protein transports vitamin A in our blood Secondary  The folding of a polypeptide chain due to hydrogen bonds at regular intervals along polypeptide backbone or skeleton  2 types -Helix -Pleated sheets  Secondary structure is protein dependent Tertiary  Bonding between side chains (R groups) of the various amino acids  R chains provide tertiary structure -Hydrophobic interactions: nonpolar side chains usually cluster at the core of the protein (out of contact with H 2) -Hydrogen bonds between tertiary structure -Ionic bonds between positively and negatively charged side chains -Disulfide bridges (strong covalent bonds) form when 2 cysteine monomers are brought close together by the folding of the protein Quaternary  Interaction of more than one polypeptide chain (or subunit)  Some proteins consist of more than one polypeptide chain  Nucleic Acids: store, transmit, and help express heredity information  The amino acid sequence of a polypeptide is programmed by a unit of inheritance called a gene  Genes consist of DNA, a nucleic acid made of monomers called nucleotides  2 types of nucleic acids -Deoxyribonucleic acid (DNA) -Ribonucleic acid (RNA)  DNA provides directions for its own replication  Gene expression: DNA directs synthesis of messenger RNA (mRNA) and, through mRNA, controls protein synthesis  The flow of genetic information: DNARNAProtein  Nucleic acids are polymers called polynucleotides  Each polynucleotide is made of monomers called nucleotides Each nucleotide consists of a nitrogenous base, a pentose sugar, and one or more phosphate group  The portion of a nucleotide without a phosphate group is called a nucleoside  Nucleoside=nitrogenous base + sugar  2 families of nitrogenous bases -Pyrimidines have a single 6-membered ring -Purines have a 6-membered ring fused to a 5-membered ring  Nucleotide=nucleoside + phosphate group  DNA molecules have 2 polynucleotides spiraling around an imaginary axis, forming a double helix  The backbones run in opposite directions from each other, an arrangement referred to as antiparallel Chapter 6 Cells  The lowest level structure capable of performing all the activities of life  Known as cytology or cell biology Prokaryotes  Bacteria  Simple structure  No membrane-enclosed organelles  Has NO nucleus  DNA is concentrated in a region called nucleoid but no membrane surrounds it  The study of bacteria=microbiology Eukaryotes  All life forms except bacteria  Includes plants, fungi, and animal cells  True karyon (or nucleus), indicates the nucleus is enclosed by a membrane  Possess membrane-bound organelles  Typically, 10X bigger than bacteria Prokaryotes vs. Eukaryotes  Prokaryotes -No nucleus, just a region in the cell containing DNA (called nuclei) -No membrane-bound organelles but has plasma membrane and ribosomes  Eukaryotes -Nucleus -Variety of organelles -Organelles have membranes Plant vs. Animal Cells  Most organelles are found in both plant and animal cells  Animal cells have the following organelles that plant cells do NOT have -Lysosomes -Centrioles -Flagella  Plant cells have the following organelles that animal cells do NOT have -Chloroplasts -Central vacuole -Cell wall plasmodesmata Nucleus  Contains most genetic material of cell  Its enclosed by the nuclear envelope -The nuclear envelope is a double membrane with pores for the passage of certain macromolecules.  Within the nucleus our DNA is organized with protein into chromatin that looks like a stringy mess with a microscope.  Chromatin condenses into chromosomes before cell division Nucleolus  Site of synthesis and assembly of the components of ribosomes  Ribosome components then pass through the nuclear pores to the cytoplasm where they combine to form ribosomes Ribosomes  Site of protein synthesis  2 types of ribosomes -Free ribosomes-suspended in the cytoplasm  They make proteins that function within the cytoplasm. -Bound ribosomes-attached to the ER  They generally make proteins that are parts of membranes or to be exported from the cell. Endoplasmic Reticulum (ER)  Endoplasm=cytoplasm; reticulum=network  A membranous network within the cytoplasm  Consists of membranous tubules and sacs called cisternae  The ER membrane separates its internal compartment from the cytosol  The ER is also continuous with the nuclear envelope  2 types of ER -Smooth -Rough Smooth ER  Cytoplasmic surface lacks ribosomes  Functions in -Lipid synthesis (fats, phospholipids, steroids) -Calcium ion storage in muscle cells Rough ER  Cytoplasmic surface of ER membrane is studded with ribosomes  Functions in the final steps of synthesizing membrane proteins  Proteins are folded into their native states within the ER Golgi Apparatus  It is the center of -Manufacturing -Sorting -Warehousing -Shipping  One side of Golgi receives transport vesicles from the ER and then ships material out from its trans face  The cis face is usually located near ER  Protein products are modified while traveling inside Golgi, from the receiving to the shipping end Lysosomes  Membrane-enclosed bag of hydrolytic enzymes  Cell uses lysosomes to digest macromolecules and part of damaged cells  Membranes are important in lysosomes, otherwise the hydrolytic enzymes would digest otherwise healthy cells Lysosome Functions  Phagocytosis: process of engulfing food particles -Performed by amoebas and in some human cells as well  Autophagy: recycling the cell’s own organic material -Lysosome engulfs another organelle (human liver does this often)


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