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anatomy

chapter 2

QuestionAnswer
solutions homogeneous, particles ARE evenly distributed through solvent
solute substance dissolves in solvent
solvent substances presented in great amounts-> liquids
colloids heterogeneous, particles are NOT evenly distributed in mixture
suspensions heterogenous, large visible solutes that DO settle out
isotopes atoms contain same number of proteins but differ in number of neutrons - atomic numbers are same, but mass number is different
radioisotopes isotopes that decompose to more stable forms. atoms loses various subatomic particles-> loss results in an isotope becoming different element.
radioactivity as isotopes decay-> subatomic particles release a little energy
ionic bonds (transfer) involve transfer of valence shell electrons from one atom to another - attractions of opposite charges result in ionic bond
anion (-), atoms that gained one or more electrons
cation (+), atoms that lost one or more electrons
covalent bonds (sharing) formed by sharing 2 or more valence shell electrons between 2 atoms
electrons in covalent bonds 2 electrons-> single bond 4 electrons-> double bonds 6-> triple bonds
elements that make up body carbon, oxygen, hydrogen, nitrogen
reduction-oxidation or redox reactions Atoms are reduced when they gain electrons and oxidized when they lose electrons Example: C6H12O6 + 6O2 → 6CO2 + 6H2O + ATP
Exergonic-net release of energy (give off energy) Products have less potential energy than reactants Catabolic and oxidative reactions
Endergonic-net absorption of energy (use up energy) Products have more potential energy than reactants Anabolic reactions
Reversibility of Chemical Reactions All chemical reactions are theoretically reversible. A + B ↔ AB. Chemical equilibrium occurs if neither a forward nor a reverse reaction is dominant .Many biological reactions are not very reversible. Energy requirements to go backward are too high, or products have been removed
Rate of Chemical Reactions The speed of chemical reactions can be affected by Temperature: increased temperatures usually increase rate of reaction Concentration of reactants: increased concentrations usually increase rate Particle size: smaller particles usually increase rate
Catalysts Catalysts increase the rate of reaction without being chemically changed or becoming part of the product Enzymes are biological catalysts
Inorganic compounds Water, salts, and many acids and bases Do not contain carbon
Organic compounds Carbohydrates, fats, proteins, and nucleic acids Contain carbon, are usually large, and are covalently bonded
Water Most abundant inorganic compound Accounts for 60%−80% of the volume of living cells Most important inorganic compound because of its properties High heat capacity High heat of vaporization Polar solvent properties Reactivity Cushioning
Salts ionic compounds that dissociate into separate ions in water Separate into cations (positively charged molecules) and anions (negatively charged)----> called electrolytes
Acids and bases are both electrolytes Ionize and dissociate in water Acids-Are proton donors: they release hydrogen bare protons (have no electrons) in solution. Important acids HCl (hydrochloric acid), HC2H3O2 (acetic acid, abbreviated HAc), and H2CO3 (carbonic acid)
bases Are proton acceptors.When a base dissolves in solution, it releases a hydroxyl ion.Important bases- bicarbonate ion
pH: Acid-base concentration pH scale is measurement of concentration of hydrogen.The more hydrogen ions in a solution, the more acidic that solution is
pH: Acid-base concentration Acidic solutions have high.Acidic pH range is 0–6.99 Alkaline (basic) solutions have low H but high PH -Alkaline pH range is 7.01–14
Neutralization Neutralization reaction: acids and bases are mixed together Displacement reactions occur, forming water and a salt NaOH + HCl → NaCl + H2O
Buffers Acidity involves only free bound to anions Buffers resist abrupt and large swings in pH Can release hydrogen ions if pH rises Can bind hydrogen ions if pH falls
buffers pt.2 Convert strong acids or bases (completely dissociated) into weak ones (slightly dissociated) Carbonic acid–bicarbonate system (important buffer system of blood):
OH- alkaline (basic) : PH range is 7.01-14
H+ very acidic:, PH range is 0-6.99
Organic molecules contain carbon Exceptions: CO2 and CO, which are inorganic
Carbon is electroneutral Shares electrons; never gains or loses them Forms four covalent bonds with other elements Carbon is unique to living systems
Major organic compounds: carbohydrates, lipids, proteins, and nucleic acids
Many are polymers Chains of similar units called monomers (building blocks) Synthesized by dehydration synthesis Broken down by hydrolysis reactions
Carbohydrates include sugars and starches Contain C, H, and O Hydrogen and oxygen are in 2:1 ratio 3 classes:Monosaccharides,Disaccharides,Polysaccharides
Monosaccharides Important monosaccharides one single sugar Monomers: smallest unit of carbohydrate Pentose sugars (Ribose and deoxyribose) Hexose sugars (Glucose (blood sugar))
Disaccharides two sugars Double sugars Too large to pass through cell membranes Important disaccharides (Sucrose, maltose, lactose) Formed by dehydration synthesis of two monosaccharides glucose + fructose → sucrose + water
Polysaccharides many sugars Polymers are made up of monomers of monosaccharides Polymers of monosaccharides Formed by dehydration synthesis of many monomers Important polysaccharides Starch: carbohydrate storage form used by plants Glycogen: carbohydrate storage form used by animals Not very soluble
lipids Contain C, H, O, but less than in carbohydrates, and sometimes contain P Insoluble in water Main types: Triglycerides or neutral fats Phospholipids Steroids Eicosanoids
lipids Triglycerides or neutral fats Called fats when solid and oils when liquid Composed of three fatty acids bonded to a glycerol molecule Main functions Energy storage Insulation Protection
triglycerides saturated fatty acid All carbons are linked via single covalent bonds, resulting in a molecule with the maximum number of H atoms (saturated with H) Solid at room temperature (Example: animal fats, butter)
lipids Unsaturated fatty acids One or more carbons are linked via double bonds, resulting in reduced H atoms (unsaturated) Liquid at room temperature (Example: plant oils, such as olive oil) Trans fats – modified oils; unhealthy Omega-3 fatty acids – “heart healthy”
lipid phospholipids Modified triglycerides Glycerol and two fatty acids plus a phosphorus-containing group
lipids phospholipids Head” and “tail” regions have different properties Head is a polar region and is attracted to water Tails are nonpolar and are repelled by water Important in cell membrane structure
lipids steroids Consist of four interlocking ring structures Common steroids: cholesterol, vitamin D, steroid hormones, and bile salts
lipids steroids Most important steroid is cholesterol Is building block for vitamin D, steroid synthesis, and bile salt synthesis Important in cell plasma membrane structure
lipids eicosanoids Derived from a fatty acid (arachidonic acid) found in cell membranes Most important eicosanoids are prostaglandins Play a role in blood clotting, control of blood pressure, inflammation, and labor contractions
Chemistry underlies all physiological reactions: Movement, digestion, pumping of heart, nervous system
matter Matter is anything that has mass and occupies space Matter can be seen, smelled, and/or felt Weight is mass plus the effects of gravity
states of matter Matter can exist in three possible states: Solid: definite shape and volume Liquid: changeable shape; definite volume Gas: changeable shape and volume
Chemical energy Stored in bonds of chemical substances Electrical energy Results from movement of charged particles Mechanical energy Directly involved in moving matter Radiant or electromagnetic energy Travels in waves (example: heat, visible light, ultraviolet light, and X rays)
4 elements in body Carbon, oxygen, hydrogen, and nitrogen
atomic number Number of protons in nucleus Written as subscript to left of atomic symbol Example: 3Li
mass number Total number of protons and neutrons in nucleus Total mass of atom Written as superscript to left of atomic symbol Example: 7Li
electron shells each shell has electrons-> certain amount of kinetic and potential energy-> depends on size , atom can have up to 7 electron shells.
electron shells pt 2 Shells can hold only a specific number of electrons; the shell closest to nucleus is filled first Shell 1 can hold only 2 electrons. Shell 2 holds a maximum of 8 electrons. Shell 3 holds a maximum of 18 electrons
Octet rule (rule of eights) Exceptions: smaller atoms (examples: H and He) want only 2 electrons in shell 1 Desire to have 8 electrons is driving force behind chemical reactions.Noble gases already have full 8 valence electrons (or 2 for He) so are not chemically reactive.
Octet rule (rule of eights) pt 2 Most atoms do not have full valence shells Atoms will gain, lose, or share electrons (form bonds) with other atoms to achieve stability of 8 electrons in valence shell
iconic bond (transfer) Ions are atoms that have gained or lost electrons and become charged Number of protons does not equal number of electrons attraction of opposite charges most are salts
colavent bonds formed by sharing of two or more valence shell electrons between two atoms Sharing of 2 electrons results in a single bond Sharing of 4 electrons is a double bond Sharing of 6 electrons is a triple bond
covalent -> nonpolar Equal sharing of electrons between atoms Results in electrically balanced, nonpolar molecules such as CO2cov
covalent-> polar Unequal sharing of electrons between 2 atoms Results in electrically polar molecules Results in electrically polar molecules Atoms have different electron-attracting abilities, leading to unequal sharing Atoms with greater electron-attracting ability are electronegative, and those with less are electropositive
polar covalent bonds H2O is a polar molecule Oxygen is more electronegative, so it exerts a greater pull on shared electrons, giving it a partial negative charge and giving H a partial positive charge Having two different charges is referred to as dipole
hydrogen bonds Attractive force between electropositive hydrogen of one molecule and an electronegative atom of another molecule Not true bond, more of a weak magnetic attraction
hydrogen bonds pt 2 Common between dipoles such as water What makes water liquid Also act as intramolecular bonds, holding a large molecule in a three-dimensional shape
Chemical reactions occur when chemical bonds are formed, rearranged, or broken These reactions can be written in symbolic forms called chemical equations Chemical equations contain: Reactants: substances entering into reaction together Product(s): resulting chemical end products Amounts of reactants and products are shown in balanced equations
Compounds are represented as molecular formulas Example: H2O or C6H12O6 or H2 or CH4 In chemical equations, subscripts indicate how many atoms are joined by bonds, whereas prefix means number of unjoined atoms (example: 4H)
synthesis (combination) reactions involve atoms or molecules combining to form larger, more complex molecule Used in anabolic (building) processes A + B → AB
decomposition reactions involve breakdown of a molecule into smaller molecules or its constituent atoms (reverse of synthesis reactions) Involve catabolic (bond-breaking) reactions AB → A + B
Exchange reactions also called displacement reactions, involve both synthesis and decomposition Bonds are both made and broken AB + C → AC + B and AB + CD → AD + CB
proteins Comprise 20–30% of cell mass Have most varied functions of any molecules Structural, chemical (enzymes), contraction (muscles) Contain C, H, O, N, and sometimes S and P
proteins Polymers of amino acid monomers held together by peptide bonds Shape and function depends on four structural levels
amino acids and peptides All proteins are made from 20 types of amino acids Joined by covalent bonds called peptide bonds
amino acids and petides Contain both an amine group and acid group Can act as either acid or base Differ by which of 20 different “R groups” is present
Structural Levels of Proteins-> 4 levels Primary: linear sequence of amino acids (order) Secondary: how primary amino acids interact with each other Alpha (α) helix coils resemble a spring Beta (β) pleated sheets resemble accordion ribbons
Structural Levels of Proteins-> 4 levels Tertiary: how secondary structures interact Quaternary: how 2 or more different polypeptides interact with each other
Fibrous and Globular Proteins -> fibrous (structural) proteins Strandlike, water-insoluble, and stable Most have tertiary or quaternary structure (3-D) Provide mechanical support and tensile strength Examples: keratin, elastin, collagen (single most abundant protein in body), and certain contractile fibers
Fibrous and Globular Proteins -> globular (functional) proteins Compact, spherical, water-soluble, and sensitive to environmental changes Tertiary or quaternary structure (3-D) Specific functional regions (active sites) Examples: antibodies, hormones, molecular chaperones, and enzymes
Protein Denaturation Denaturation: globular proteins unfold and lose their functional 3-D shape Fibrous proteins are more stable Active sites become deactivated
Protein Denaturation Can be caused by decreased pH (increased acidity) or increased temperature Usually reversible if normal conditions restored Irreversible if changes are extreme Example: cannot undo cooking an egg
Enzymes and Enzyme Activity Enzymes: globular proteins that act as biological catalysts Catalysts regulate and increase speed of chemical reactions without getting used up in the process
enzymes Lower the energy needed to initiate a chemical reaction Leads to an increase in the speed of a reaction Allows for millions of reactions per minute!
Enzymes and Enzyme Activity Most functional enzymes, referred to as holoenzymes, consist of two parts Apoenzyme (protein portion) Cofactor (metal ion) or coenzyme (organic molecule, often a vitamin)
Enzymes and Enzyme Activity Enzymes are specific Act on a very specific substrate Names usually end in –ase and are often named for the reaction they catalyze Example: hydrolases, oxidases
Enzymes and Enzyme Activity Enzymes lower activation energy, which is the energy needed to initiate a chemical reaction Enzymes “prime” the reaction Enzymes allow chemical reactions to proceed quickly at body temperatures
Enzymes and Enzyme Activity Three steps are involved in enzyme action: Substrate binds to enzyme’s active site, temporarily forming enzyme-substrate complex Complex undergoes rearrangement of substrate, resulting in final product Product is released from enzyme
Nucleic Acids Nucleic acids, composed of C, H, O, N, and P, are the largest molecules in the body Nucleic acid polymers are made up of monomers called nucleotides Composed of nitrogen base, a pentose sugar, and a phosphate group
Nucleic Acids Two major classes: Deoxyribonucleic acid (DNA) Ribonucleic acid (RNA)
Nucleic Acids DNA holds the genetic blueprint for the synthesis of all proteins Double-stranded helical molecule (double helix) located in cell nucleus
Nucleic Acids Nucleotides contain a deoxyribose sugar, phosphate group, and one of four nitrogen bases: Purines: adenine (A), guanine (G) Pyrimidines: cytosine (C) and thymine (T)
Nucleic Acids DNA holds the genetic blueprint for the synthesis of all proteins Bonding of nitrogen base from strand to opposite strand is very specific Follows complementary base-pairing rules: A always pairs with T G always pairs with C
Nucleic Acids RNA links DNA to protein synthesis and is slightly different from DNA Single-stranded linear molecule is active mostly outside nucleus Contains a ribose sugar (not deoxyribose)
nucleic acid Thymine is replaced with uracil Three varieties of RNA carry out the DNA orders for protein synthesis Messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA)
ATP Chemical energy released when glucose is broken down is captured in ATP (adenosine triphosphate) ATP directly powers chemical reactions in cells Offers immediate, usable energy needed by body cells Structure of ATP Adenine-containing RNA nucleotide with two additional phosphate groups
ATP Phosphorylation Turns on reactions Terminal phosphate group of ATP can be transferred to other compounds that can use energy stored in phosphate bond to do work Loss of phosphate group converts ATP to ADP Loss of second phosphate group converts ADP to AMP
Created by: lunagmia
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