exam 1 study guide
exam 1 study guide BIOL 2107
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This 3 page Study Guide was uploaded by Alexandra Irvin on Tuesday September 13, 2016. The Study Guide belongs to BIOL 2107 at Georgia Southern University taught by Lace Svec in Summer 2016. Since its upload, it has received 4 views. For similar materials see principles of biology I in Biology at Georgia Southern University.
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Date Created: 09/13/16
PRINCIPLES OF BIOLOGY EXAM 1 STUDY GUIDE When two hydrogen bonds run into each other o Hydrogen has one valence electron=very unstable o High potential energy because electrons are being pulled at any given time. o Have a chance to share and fill valence shells. o Electrons go back and forth between the two atoms trying to accomplish a full shell. o Nonpolar covalent bond which allows the atom to remain uncharged; share electrons equally. o Being held together by: filling orbitals and the attraction between electrons and protons in two atoms. When hydrogen and oxygen run into each other + o Oxygen has high electronegativity which means oxygen is winning the “tug of war” concerning hydrogens electron. o Oxygen has an extra electron; hydrogen has one less electron = partial charges. o Polar covalent bond o Lower potential energy because oxygens electronegativity is so much greater than hydrogens. Type of bonds: o Covalent=strong bond o Ionic=weak bond o Hydrogen=weak bond (stronger than vdW interaction; intermolecular) o Van der Waals=weakest bond van der Waals interactions: weak attractions between molecules or parts of molecules that result from transient local partial charges. o Always occurs in hydrocarbon molecules Ions: charged particles; positive or negative symbol on an atom. (ex: H , Ca , [OH]) o Partial charges in structural formula polar covalent bonds are NOT symbolized. Organic molecules: presence of carbon and hydrogen is almost always true; often called a carbon skeleton. o Carbon and hydrogen bond are symbolized by a o The endpoints and branches on symbol are carbon molecules, the hydrogens are assumed and don’t need to be symbolized or written. Functional groups: projecting from the carbon skeleton of structural formulas; on the outside and are the interacting elements. o Hydroxyl C—OH o Carbonyl C==O O o Carboxyl C ==OOH == o Amino CNH 2 C—O--P— o Sulfhydrl CSH OH o Phosphate --- o OH o Methyl CCH3 Macromolecules: are made up of monomers Monomers are small units with similar characteristics that join to form larger molecules. Monomers come together to form polymers by repeating units held together by covalent bonds. This is known as polymerization Macromolecules have four classes: carbohydrates, lipids, nucleic acids and proteins. Carbohydrates o Used to transport and store energy, mostly used for fuel. o Also used to build structures. (ex: in plants carbohydrates make up cellulose) o Carbohydrates are made up of monomers known as saccharides, a few of which are glucose, fructose and lactose. Characteristics of saccharides: contain many hydroxyl groups and a carbonyl group; you can look for a 1:2:1 ratio of carbon, hydrogen, oxygen (CH O2; you can look for a “ring” structure The bond that holds saccharides together in a polysaccharide is a covalent glycosidic bond. Lipids o Hydrophobic and made of hydrocarbons o There are three classes of lipids: fats, steroids and phospholipids. Fats can be identified by a fatty acid tail Steroids can be identified by four fused hydrocarbon rings Phospholipids can be identified by a fatty acid tail as well as a phosphate group Nucleic Acids o Typically found in a long, linear structure and in molecules that hold information (ex: RNA, DNA). o Made up of monomers known as nucleotides Nucleotides have 3 primary parts: a phosphate group covalently bonded to a saccharide and a nitrogenous base (T, C, G, A). Saccharides found are usually deoxyribose and ribose. Proteins o Regulate chemical reactions, transport within the cell, act as signaling molecules, act as receptors for those signals, protection for the cell in the form of antibodies, control movement of the cell, and is the basic structure of the cell. Proteins have a wide range of structures but some examples of where they can be found are: in a fibrous structure (long, stringlike), globular structure (ball or clump) and structures with in the membrane (can be gate like). o Made of amino acid monomers. o You can recognize an amino acid by looking for an amino group and a carboxyl group around a central carbon and an R group, or side chain. o Amino acids joined by a bond between the carboxyl group and the amino group form a polypeptide This is a dehydration reaction Bond between two amino acids is known as a peptide bond Polypeptide is made up of the backbone (amino group and carboxyl group) and side chains (depends on which amino acid is added). o The levels of structure in a protein are: helix or pleated sheet, to tertiary structure and then to quaternary structure.
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