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chemistry///

QuestionAnswer
are atoms of the same element with different numbers of neutrons. Isotopes
The mass number of an atom is a sum of the protons and neutrons in the atoms nucleus.
The atomic mass of an element is the average of all the existing isotopes for that element.
If you change the number of electrons . . . an ____ is formed an ion is formed.
– atom with a charge Ion
two types of ions anions & cations
Negatively Charged Ions - formed by gaining electrons - the tendency of an atom to attract electrons to itself is its electron affinity anions
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
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
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
More than one pair of electrons can be shared. 1 pair = single bond 2 pairs = double bond 3 pairs = triple bond covalent bonding
When atoms do not share electron pairs equally, a polar covalent bond results. Polar Covalent Bonding
These molecules will have a slightly positive end and a slightly negative end. polar covalent bonding
• Red Spheres – Hydrogen atoms – Positive charge • Blue Spheres – Oxygen atoms – Negative charge Hydrogen Bonding
A pure substance that is made of more than one element is called a compound. compounds
can be broken down into simpler substances Compounds
is the smallest particle of a compound that has all the properties of that compound. A molecule
gain of electrons anions
loss of electrons cations
• 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
• 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
• 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
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
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
is a measure of the amount of hydrogen ion in solution pH scale
0-7 is Acidic
7 is Neutral
7-14 is Basic
• compounds containing large amounts of carbon Organic Compounds
carbon forms 4 covalent bonds forming chains, rings and other structures organic compounds info
4 macromolecules unique to living things: carbohydrates, lipids, proteins, nucleic acids
- the making of proteins and large carbohydrates by removing water from two smaller molecules Dehydration synthesis
- “water splitting” Hydrolysis reactions
•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
• Disaccaharide- 2 simple sugars –Ex: sucrose, lactose Carbohydrates
• 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
• 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
– single covalent bonds between carbon atoms saturated fats
– double bonds between atoms unsaturated fats
is accomplished by attaching 3 fatty acids to a single glycerol molecule = triglycerides fat synthesis
• 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
• flat molecule made of 4 interlocking hydrocarbon rings • cholesterol – needed for cell membranes and raw material of vitamin D, steroids and bile salts Steroids
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
• 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
2 nucleic acid types dna and rna
- deoxyribonucleic acid- nucleus, contains T, info for living things, contains deoxyribose sugar, double stranded dna
- ribonucleic acid- cytoplasm, contains U, protein synthesis, contains ribose sugar, single stranded, 3 types: mRNA, rRNA, tRNA rna
nucleotides are held together by ??? –A–T (inRNA A–U) –G–C hydrogen bonds
• macromolecules made of linked amino acids (AA) • basic structural material of the body Proteins
• 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
• 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
protein structures primary structure, secondary structure, tertiary structure, and quaternary structure.
- the linear AA sequence primary structure
secondary structure- 2 types a helix and B pleated sheats
- coils like a telephone cord – α helix
- ribbon like structure hydrogen bonds stabilize the proteins β pleated sheets
α helix or β pleated regions of the chain fold upon one another to produce ball-like molecules tertiary structure-
- 2 or more chains aggregate in a regular manner to form a complex protein quaternary structure
• 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
• compact, spherical proteins with tertiary structure and some have quaternary structure • water soluble • chemically active • Ex: antibodies, enzymes Globular or Functional Proteins
•proteins that act as biological catalysts •enzymes are chemically specific Enzymes
•enzymes determine if reactions will occur •enzymes have the suffix –ase and are named for the reaction they catalyze enzymes
•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
Created by: a.quimbaya1