Docsity
Docsity

Prepare for your exams
Prepare for your exams

Study with the several resources on Docsity


Earn points to download
Earn points to download

Earn points by helping other students or get them with a premium plan


Guidelines and tips
Guidelines and tips

Exam 1 Notes - Chemical Bonds, Ionic and Covalent Bonds | BIOL 1201, Study notes of Biology

Exam 1 Notes Material Type: Notes; Professor: Siebenaller; Class: BIOL FOR SCI MAJ I; Subject: Biological Sciences; University: Louisiana State University; Term: Spring 2011;

Typology: Study notes

2010/2011

Uploaded on 05/11/2011

ginamarie2010
ginamarie2010 🇺🇸

5

(1)

1 document

1 / 19

Toggle sidebar

Related documents


Partial preview of the text

Download Exam 1 Notes - Chemical Bonds, Ionic and Covalent Bonds | BIOL 1201 and more Study notes Biology in PDF only on Docsity! January 20, 2011 Moodle Quiz 1 after today’s lecture – before class on Tuesday CHEMICAL BONDS Strong  Covalent bonds involve sharing of electrons  Hydrogen (H2)  Oxygen (O2) o Water (H2O) o Methane (CH4) Weak  Non-covalent bonds o Ionic interactions – attraction of opposite charges. One atom donates an electron to another o Hydrogen bond between partially charged atoms VALENCE VS. VALENCE ELECTRONS  Valence is the number of electrons needed to fill the outermost shell of an atom o Hydrogen valence = 1 o Oxygen valence = 2  Valence electrons are the electrons contained in the outermost electron shell of an atom MOLES AND MOLAR CONCENTRATION  1 Mole = the mass of a substance equal to its gram molecular weight  1 Molar solution = a solution containing 1 mole of a substance per 1 liter of solution Can you have a 1 Molar solution of insulin? No  5.727 kg/liter or 5.727 g/cm3 IONIC BONDS  Weak bond  Transfer of an electron from one atom to another o NaCl = Na+ and Cl- COVALENT BONDS  Strong bond  Sharing of electrons to complete valence shell o Water (H20): polar covalent with 104.5° angle, so the Hydrogens have a partial positive charge and the oxygen has a partial negative charge (partial charges represented by lower case delta) POLAR BONDS  Unequal sharing of electrons  Partial + and partial – regions  No net charge HYDROGEN BONDS  Weak (non-covalent) bonds  Between partial positive and partial negative charges o Water (H20) and Ammonia (NH3); weak bond between the hydrogen and nitrogen WATER  70 to 90% of weight of most life forms  Sets the lower temperature limit for life  Sets the upper temperature limit? (Probably not) o How quickly biological molecules break down in high temperatures  Important role in structures and properties of biological molecules  Water is a biological molecule THE UNUSUAL PROPERTIES OF WATER  Result from hydrogen bonding  Water behaves as a much larger molecule BONDS  Covalent: H-O 110 kcal per mole  Angle 104.5°  Weak (hydrogen bond): 4.5 kcal/mol o H bonding effectively makes water a larger molecule o In ice a water molecule interacts with exactly 4 other water molecules o In liquid water, on average 3.6 or fewer other molecules (can be made and broken very quickly) SMALL MOLECULES – A COMPARISON OF PROPERTIES  Water – H20 o BP: 100°C o FP: 0°C  Ammnonia – NH3 o BP: 35°C o FP:-37°C  Ethanol – o BP: 78.5°C o FP: -117.3° UNUSUAL PROPERTIES OF WATER  High heat capacity o Amount of heat to raise temperature of 1 g of water by 1°C o 1 cal per g of water  High heat of vaporization o Amount of heat to vaporize 1 g of water o 540 cal per g at 100°C  High heat of fusion o Amount of heat removed to freeze 1 g of water o 80 cal per g CARBOHYDRATES  General formula (CH2o)n o E.g., n = 6 o C6H12O6  Also are sugars, monosaccharides  Ring structures & linear structures  Disaccharide – loses 2 H and 1 O (H2O)  Starch in plants; Glycogen in animals – polymers of glucose  Energy roles o Metabolic fuel  Glucose  Sucrose o Storage form  Starch (plants)  Glycogen (animals)  Structural roles o Cellulose (in plants)  Monomer of glucose o Chitin (animals)  Polymer of glucose  Exoskeleton of insects LIPIDS  Water-insoluble organic biomolecules made up of “non-polar” groups o Due to their nonpolar groups  Structural components of cell membrane  Storage and transport form of fuel  Protective surface coating o E.g. leaves  Cell component in cell recognition  Hormone  Hydrophobic FAT TYPES  Saturated o Saturated with H, no double bonds between adjacent carbons o Bad because they raise LDL cholesterol  Unsaturated o Double bonds, lower melting point o The “good” fat o “better” than saturated fats MELTING POINTS DIFFER  Saturated fats are solids at higher temperatures than unsaturated fats  Acyl chains of unsaturated fats are kinky and therefore require a lower temperature to become solid POLYMERS  Triglycerides o Components: glycerol and three fatty acids  Phospholipids o Phospholipid bilayer COMPARISON OF LIPIDS AND CARBOHYDRATES  Twice as much energy from fat  Stored without water  1 g of glycogen is store with 2 to 5 g of water  (Disadvantage – not as rapidly mobilized as carbohydrates)  lipids metabolized in the mitochondria in the presence of O2 The hump of camel is filled with lipid. CAMEL  Up to 20% of body mass is fat when food is plentiful  Subcutaneous fat would cause thermoregulatory problems BEAR  Hibernation 100 days without eating o Due to accumulated fat HUMAN  Normal weight – 40 day reserve of energy  Moderately obese – up to a year NUCLEIC ACIDS  Nitrogenous heterocyclic bases  Pentose sugar (5C)  Phosphoric acid  Examples: o Coenzymes (NAD, NADP, FAD) o Genetic material (DNA and RNA) o ATP PROTEINS  Excellent example of a polymer  Made of amino acids o 20 naturally occurring amino acids are L-isomers o Proteins vary in the number and sequence of the different kinds of amino acids ENZYMES  Protein catalyst  Every chemical reaction in a living cell is catalyzed by a specific enzyme STORAGE PROTEIN  Seed  Eggs CONTRACTILE PROTEINS  In muscle  Actin  Myosin DEFENSIVE BLOOD PROTEINS  Antibodies TOXINS  For example from bacteria  Pertussis toxin  Botulinum toxin HORMONES AND RECEPTORS  Hormones – chemical messengers o E.g. insulin  Receptors – specific recognition sites for chemical messengers STRUCTURAL PROTEIN o Hair o Silk AMINO ACIDS  The monomers  20 kinds AMINO ACID STRUCTURE  Central Carbon  Amino group (NH2)  Carboxyl group (acid) (COOH)  Hydrogen  R group (20 different R groups) NOTE THERE ARE DIFFERENT TYPES OF R GROUPS  Polar (hydrophilic) o Can be electrically charged R groups o Interact with the partial + and – charges of water  Non-polar (hydrophobic) o No partial charges on the R group  Charged ( + or - ) THE CHARACTERISTICS OF THE INDIVIDUAL AMINO ACIDS DETERMINE THE STRUCTURE OF THE PROTEIN Saturated fats have higher melting points. COVALENT BOND BETWEEN AMINO ACIDS  Peptide bond  Dehydration synthesis THE PEPTIDE BOND  Does not involve the R groups  The amino and carboxyl groups (common to all amino acids) are involved PRIMARY STRUCTURE  Sequence of amino acids in a protein or peptide  Determines what the protein will look like and how it functions 80,000 Americans have sickle cell disease 2.5 million express sickle trait SECONDARY STRUCTURE  4 suspected cases alive in the UK  6 of the other 48 cases worldwide resided in the UK for some time  In US  3 cases  all epidemiologically linked to cattle product contaminated with BSE CHRONOLOGY IN THE UK  1970s – mid 1980s spread from sheep to cattle o sheep meat and bones aadded to cattle feed o 1982 Prusiner discovers prions o 1986 Mad cow disease indentified o in 10 years 165,000 cattle affected o November 1989 British government banned use of animal- derived feed supplements o March 1996 EU bans British beef BANNED FEED  Sold in Europe and Asia  Sold for “use” in poultry  vCJD in Great Britain and France o All but one of vCJD patients younger than 40 years old UNUSUAL DISEASES  Not caused by “germs”  Not a virus, bacteria, or fungus  Not caused by organism with genetic material!  However – this is still controversial PRIONS  Proteinaceous Infectious Particles  Discover in 1982 by Stanley Prusiner o Nobel Prize in 1987 February 1, 2011 BSE IN US  December 2003  Discovered in “downer” dairy cow in the state of Washington NORMAL CELLULAR FORM OF THE PRION PROTEIN  Alpha helix o Present in all mammals o May protect neurons from toxic copper ions DISEASE FORM  Beta-pleated sheet o Resistant to most denaturation techniques SAME AMINO ACID SEQUENCE!  Different secondary structures  Disease form converts the normal cellular form to the beta pleated sheet protein  Secondary structure o Important in determining the role/function of the protein Mad cow disease was spread by contaminated feed – true! Eating beef from “mad cows” may result in vCJD. The normal protein and the disease causing prion differ in the secondary structure. CELLS: STRUCTURE AND FUNCTION PROBLEMS  Increase size means relatively less surface area for a unit of volume  This causes a problem with movement of materials into and out of the cell  A second problem is controlling and coordinating metabolic processes within the cell OVERVIEW – CELL STRUCTURE  Keeping cell distinct from the environment  Organizing and coordinating metabolic processes THREE DOMAINS  Bacteria  Archaea  Eukarya WE’LL USE TWO CATEGORIES BASED ON STRUCTURAL FEATURES  Prokaryotes o Archaea o Eubacteria  Eukaryotes o Eukarya PROKARYOTES  “Before” the nucleus  No internal membrane-bound organelles EUKARYOTES  “True” nucleus  Have organelles bounded by membranes PROKARYOTES (BACTERIA AND BLUE-GREEN ALGAE) 1. Cell wall of carbohydrates and peptides 2. Ribosomes differ from Eukaryotes in size and antibiotic sensitivity 3. No nucleus or linear (histone-complex) chromosomes 4. No internal membranes EUKARYOTES (ANIMALS, PLANTS, FUNGI, YEASTS)  Larger cell size o Need increased internal membranes o Problem of intake of nutrients o Problem of coordinating and control of metabolism o More opportunities as a heterotroph Prokaryote Animal Plant Plasma Membrane + + + Cell Wall + - + Nucleus - + + DNA Circular Linear Linear Ribosomes Smaller Larger Larger ER - + + Gogli - + + Lysosomes - + + Vacuoles - Small or absent Large, one Mitochondria - + + Chloroplasts - - + 9+2 Flagella - + Not higher plants Plants and animals are Eukaryotes. PLASMA MEMBRANE  Present in Prokaryotes and Eukaryotes  Semi-fluid mosaic  Phospholipids  Proteins  Semi-permeable barrier between contents of cell and environment A phospholipid consists of a hydrophobic tail and hydrophilic head NUCLEUS  Present in eukaryotes  Enclosed by nuclear envelope – a double membrane with pores  Contains linear chromosomes  Contains nucleolus – region of nucleus where ribosomal subunits are assembled GENETIC MATERIAL IN EUKARYOTES  Liner strands of DNA complexed with proteins (histones)  Linear chromosomes GENETIC MATERICAL IN PROKARYOTES  Circular strands of DNA  “Naked” – not complexed with histone proteins NUCLEOLUS  Region of the nucleus where ribosomal subunits are assembled RIBOSOMES  Present in eukaryotes and prokaryotes  Differ in size (prokaryotes have smaller ribosomes) and antibiotic susceptibility  Consist of two subunits  Subunits made of rRNA and protein  Site of protein synthesis  Occur free in cytoplasm of in association with the rough ER ENDOMEMBRANE SYSTEM  Endoplasmic Reticulum (ER) o Eukaryotes only o Internal membrane system  Initially cytoplasm (ground substance) was thought to be without structure o Improved techniques showed this to be wrong FLAGELLA AND CILIA  Organelles involved in movement  Bacteria have “flagella” but are constructed differently than in eukaryotes  Same structural design in flagella and cilia  9+2 structure – only in eukaryotes (absent in higher plants) o Different than the flagella of bacteria  Flagella larger and fewer in number than cilia Other elements involved in movement  Sliding filaments o Proteins involved in movement  E.g. actin and myosin  Molecular motors o Proteins o Use ATP  Centriole o In animals (but not higher plants) o Similar to the base of a flagellum of cilium o Involved in mitosis and meiosis THE PROBLEM  The interior of a cell is different than it’s environment  How to defend the internal environment but still communicate with the external environment o Transport materials across the barrier Biological membranes consist of phospholipids and proteins. INTEGRAL MEMBRANE PROTEINS  Amiphipathic o Hydrophobic (nonpolar) regions o Hydrophilic (polar) regions AN OPTIMAL INTERMEDIATE “FLUIDITY”  Not too solid  Not too fluid  Preserves membrane function  At the cell/body temperature o Similar fluidity in different species o Species with a body temperature of 10 ° C will have fluidity similar to a species with a body temperature of 20° C  (Do not take “fluidity” too literally) The fluidity of membranes of a 10°C species and a 20°C are compared to 15°C.The membranes adapted to 10° will be more fluid. HENRIQUE AND HANSEN 1901  Raised pigs wearing underwear in a hot room  Change the properties of subcutaneous fats o Had a higher melting point  Membrane fluidity can acclimate  Membrane fluidity adjusted by changing the ratio of unsaturated to saturated fatty acids To make a membrane more fluid you would increase unsaturated fats because they have a lower melting point and are more disorganized. INCREASE UNSATURATED FATS o Increases the fluidity of the membrane What kind of molecules would pass through a membrane, i.e. phospholipid bilayer? Nonpolar and small o Examples: o Gases o Steroid hormones o Water DIRECTION OF MOVEMENT o Expect – down from high concentration to low o What about against the gradient? o E.g. Sodium 5 – 15 MM in the cell; 145 mM outside the cell TRANSPORT PROCESSES o Active o Against the concentration gradient o Requires supplied energy (ATP) o Carrier molecule o Work must be done o Passive o Down concentration gradient o Does not require supplied energy o Diffusion (simple or facilitated) SIMPLE DIFFUSION o Down concentration gradient o Depends on molecular movement o Does not require supplied energy o Does not use a carrier molecule FACILITATED DIFFUSION o Down concentration gradient o Depends on molecular movement o Does not require supplied energy o Employs a carrier molecule When solute concentrations are equal on both sides of the diffusion barrier the molecules no longer move -- False o Molecules keep moving o There is no net change in solute concentration SEMI-PERMEABLE BARRIER o Only some types of molecules pass through February 7, 2011 Review session tonight 5:30 A101 Life Sciences building DIFFUSION  Movement of molecules down concentration gradient  From regions of high concentration to low concentration regions [Active transport requires energy and employs a carrier molecule Passive transport is movement down a concentration gradient and may employ a carrier molecule.] MOVEMENT OF WATER ACROSS MEMBRANES  From high to low water potential Create free energy gradients: these can be used to do work  How does the membrane allow the creation of a free energy gradient?  What is the relative free energy of molecules at different concentrations? The molecules on the left have greater free energy because they are in higher concentration. MEMBRANE PERMEABILITY  Size and shape of molecules  Solubility in lipids  Net electric charge  Other chemical properties  Water always freely permeable  Aquaporins – channel protein which facilitate water diffusion through the membrane DIFFUSION  Physical property of matter  Individual molecules move randomly, but the net effect is non-random  What forces causes the net movement? o Kinetic energy associated with the molecules OSMOSIS  The net movement of water across (through) a semi-permeable membrane.  Diffusion of water  From higher (fewer solutes) water potential to lower water potential o Fresh water has higher water potential Which way will water flow? To the right (the higher sugar concentration) PROBLEMS CONFRONTING ORGANISMS  What if the concentration of solutes differs between the intracellular compartment and the environment? HYPERTONIC  Lower water potential  More solutes dissolved
Docsity logo



Copyright © 2024 Ladybird Srl - Via Leonardo da Vinci 16, 10126, Torino, Italy - VAT 10816460017 - All rights reserved