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chemistry///

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Answer
are atoms of the same element with different numbers of neutrons.   Isotopes  
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The mass number of an atom is a   sum of the protons and neutrons in the atoms nucleus.  
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The atomic mass of an element is   the average of all the existing isotopes for that element.  
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If you change the number of electrons . . . an ____ is formed   an ion is formed.  
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– atom with a charge   Ion  
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two types of ions   anions & cations  
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Negatively Charged Ions - formed by gaining electrons - the tendency of an atom to attract electrons to itself is its electron affinity   anions  
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Positively Charged Ions - formed by losing electrons - process of removing electrons from an atom is called ionization - the energy it takes to remove the electron is the ionization energy   cations  
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occurs when atoms gain and lose electrons to form ions. Once ions are formed, a positive ion and negative ion attraction forms and creates a chemical bond.   Ionic Bonding  
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occurs when atoms share electrons to fill their outer energy levels – Usually occurs between atoms with high ionization energies and atoms with high electron affinities.   Covalent bonding  
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More than one pair of electrons can be shared. 1 pair = single bond 2 pairs = double bond 3 pairs = triple bond   covalent bonding  
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When atoms do not share electron pairs equally, a polar covalent bond results.   Polar Covalent Bonding  
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These molecules will have a slightly positive end and a slightly negative end.   polar covalent bonding  
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• Red Spheres – Hydrogen atoms – Positive charge • Blue Spheres – Oxygen atoms – Negative charge   Hydrogen Bonding  
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A pure substance that is made of more than one element is called a compound.   compounds  
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can be broken down into simpler substances   Compounds  
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is the smallest particle of a compound that has all the properties of that compound.   A molecule  
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gain of electrons   anions  
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loss of electrons   cations  
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• Produce hydrogen ions in solution (Acids usually begin with a hydrogen, HCl, HNO3) – H+ is attracted to water to form H3O+ (hydronium ions) – Make good electrolytes because of the hydrogen ions (conduct electricity)   Acids  
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• Produce hydrogen ions in solution (Acids usually begin with a hydrogen, HCl, HNO3) – H+ is attracted to water to form H3O+ (hydronium ions) – Make good electrolytes because of the hydrogen ions (conduct electricity)   Acids  
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• Sour in taste • Litmus paper (indicator paper) turns red • React with metals to form hydrogen gas and a metal compound • Corrosive • Can be described as a proton donor   acids  
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Produce hydroxide ions in solution – OH- is produced – Strong bases make good electrolytes because of the hydroxide ions (conduct electricity) – Weak bases do not make good electrolytes   bases  
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Bitter in taste • Slippery to touch • Litmus paper (indicator paper) turns blue • Corrosive & Sometimes Poisonous • The process of making soaps is called saponification • Can be described as a proton acceptor   bases  
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is a measure of the amount of hydrogen ion in solution   pH scale  
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0-7 is   Acidic  
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7 is   Neutral  
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7-14 is   Basic  
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• compounds containing large amounts of carbon   Organic Compounds  
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carbon forms 4 covalent bonds forming chains, rings and other structures   organic compounds info  
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4 macromolecules unique to living things:   carbohydrates, lipids, proteins, nucleic acids  
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- the making of proteins and large carbohydrates by removing water from two smaller molecules   Dehydration synthesis  
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- “water splitting”   Hydrolysis reactions  
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•Contain C, H, and O in a 2 H : 1 O ratio • Have a low structural use and are classified by size and solubility Types • Monosaccharide- simple sugars of 3 to 7 carbon atoms – Ex: glucose, fructose   Carbohydrates  
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• Disaccaharide- 2 simple sugars –Ex: sucrose, lactose   Carbohydrates  
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• Polysaccharide- many simple sugars –Starch- storage carb formed by plants –Glycogen- storage carb formed by animals • source of cellular fuel • excess carbs are stored as glycogen or fat   Carbohydrates  
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• Lipids- a macromolecule that contains C, H and O • non-polar substances, so they are insoluble in water • complex lipids may contain phosphorus • Ex: phospholipids, steroids, neutral fats   Lipids  
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– single covalent bonds between carbon atoms   saturated fats  
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– double bonds between atoms   unsaturated fats  
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is accomplished by attaching 3 fatty acids to a single glycerol molecule = triglycerides   fat synthesis  
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• modified triglycerides with a phosphorus containing group and 2 fatty acid chains – fatty acid chains are non-polar = water hating – phosphorus containing part is polar = water loving   Phospholipids  
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• flat molecule made of 4 interlocking hydrocarbon rings • cholesterol – needed for cell membranes and raw material of vitamin D, steroids and bile salts   Steroids  
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made of nucleotides with C, H, O, N & P – 3 parts of a nucleotide • a phosphate group • a pentose sugar • a nitrogen containing base   Nucleic Acids  
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• a nitrogen containing base – adenine (A)- purine, lg. 2 ring base – guanine (G)- purine, lg. 2 ring base – cytosine (C)- pyrimidine, sm. 1 ring – thymine (T)- pyrimidine, sm. 1 ring – uracil (U)- pyrimidine, sm. 1 ring   nucleic acids info  
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2 nucleic acid types   dna and rna  
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- deoxyribonucleic acid- nucleus, contains T, info for living things, contains deoxyribose sugar, double stranded   dna  
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- ribonucleic acid- cytoplasm, contains U, protein synthesis, contains ribose sugar, single stranded, 3 types: mRNA, rRNA, tRNA   rna  
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nucleotides are held together by ??? –A–T (inRNA A–U) –G–C   hydrogen bonds  
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• macromolecules made of linked amino acids (AA) • basic structural material of the body   Proteins  
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• enzymes- proteins that act as catalysts • most varied functions of any molecule in the body • the structure of a protein determines its biological function • classified as fibrous or globular   proteins  
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• there are 20 AA • 2 functional groups: amine group (-NH2) and organic acid group (-COOH) • can act as a base or acid • AA are combined by peptide bonds • <50 AA linked together = polypeptide   Amino Acids  
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protein structures   primary structure, secondary structure, tertiary structure, and quaternary structure.  
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- the linear AA sequence   primary structure  
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secondary structure- 2 types   a helix and B pleated sheats  
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- coils like a telephone cord   – α helix  
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- ribbon like structure hydrogen bonds stabilize the proteins   β pleated sheets  
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α helix or β pleated regions of the chain fold upon one another to produce ball-like molecules   tertiary structure-  
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- 2 or more chains aggregate in a regular manner to form a complex protein   quaternary structure  
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• extended and strandlike; most exhibit only secondary structure, but some have quaternary structure • insoluble in water • stable- provide mechanical support and tensile strength to body tissues • Ex: collagen, keratin, elastin   Fibrous or Structural Proteins  
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• compact, spherical proteins with tertiary structure and some have quaternary structure • water soluble • chemically active • Ex: antibodies, enzymes   Globular or Functional Proteins  
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•proteins that act as biological catalysts •enzymes are chemically specific   Enzymes  
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•enzymes determine if reactions will occur •enzymes have the suffix –ase and are named for the reaction they catalyze   enzymes  
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•functional proteins are called holoenzyme- made of 2 parts: apoenzyme (protein portion) and a cofactor (ion or metal). If a cofactor is derived from vitamins is called a coenzyme.   enzymes info  
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