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Midterm Review

컨트롤 버튼이 '내비게이션' 모드로 변경되었습니다.
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  • matter


    anything that has mass or occupies space

  • chemistry


    study of matter and it's interactions

  • protons


    positively charged and reside in central core of atom, the atomic nucleus

  • neutrons


    slightly larger than protons, neutral and reside in atomic nucleus

  • electrons


    surround atomic nucleus, tiny, negatively charged

  • Proton, electron balance


    protons and electrons are equal to keep atoms neutral

  • Bulk of atom


    comes from protons and neutrons- 99.5% of mass is in nucleus

  • Atomic number


    characteristic number or protons

  • 4 elements that make of most of body mass


    oxygen, carbon, hydrogen and nitrogen

  • 7 main mineral elements in body


    sodium, potassium, calcium, chorine, magnesium, phosphorous, sulfur

  • Mass number


    neutrons+protons

  • Isotopes


    atoms with same atomic number but different mass number

  • Radioisotopes


    certain unstable and high energy isotopes release energy in the form of radiation (radioactive decay) to assume a more stable form

  • Suspension


    liquid mixed with solid, solids will settle

    ex- blood

  • Colloids


    solids not visible with naked eye

    particles are suspended and do not settle

    ex- milk

  • Solutions


    solid, liquid, gas mixed with a liquid

    component dissolves

    water is most important solvent

    ex- glucose and water

  • Concentration


    amount of solute present

  • Chemical bond


    an energy relationship between atoms (attractive forces)

  • compound


    2 or more atoms of different elements bonded, called molecules of a compound

  • macromolecules


    large compounds composed of many atoms

  • valence shell


    outermost shell ( electron ring)

  • valence electrons


    electrons in outermost electron ring (valence shell)

  • octet rule


    atom is most stable when it has 8 electrons in valence shell (dont forget about duet rule though)

  • ionic bond


    electrons are transferred between a metal and a nonmetal (exception is hydrogen)

  • Covalent bond


    sharing electrons between two or more nonmetals (much more stable than ionic)

  • nonpolar covalent bond


    two nonmetals in a molecule have same electronegativity and tug on electrons with the same force until electrons are shared equally

  • polar covalent bonds


    nonmetals of different electronegativities pull on electrons and the nonmetal that is more electronegative "wins" but only partially

    winning atom isn't strong enough to completely take the electrons, they are just shared unequally

  • dipole


    two opposite poles- polar covalent bonds

    one side is slightly negative

    one side is slightly positive

  • potential and kinetic energy


    potential- stored energy

    kinetic- energy in motion

  • forms of energy in body


    chemical energy

    electrical energy

    mechanical energy

    they may all be potential or kinetic

  • endergonic reaction


    require chemical, electrical or mechanical energy from another source, produces more energy than reactants because energy was invested

  • exergonic reaction


    reactants have more energy than product, excess energy stored in reactants released during reaction

    reactants become more stable when energy is released

  • catabolic reaction


    also called decomposition breakdown

    larger substance breaks down (required to break down foods, break down old or damaged cells, defend body against invading organisms)

    AB-> A+B

  • exchange reactions


    one or more atoms from reaction are exchanged for another, bonds are broken and formed

    AB+CD-> AD+BC

  • redox reaction


    electrons are exchanged instead of atoms

    reactants that lose electrons = oxidized

    reaction that gains electrons= reduced

    generally exergonic and release lots of energy

  • Anabolic reaction


    reactions that create new chemical bonds (synthesis reactions)

    A+B-> AB

  • energy that chemical reactions require to overcome repulsion of atoms electrons


    activation energy

  • factors that increase rate of reaction by reducing activation energy or increasing chance of strong collision


    concentration

    temp

    properties of reactants (size/state)

    presence/absence of catalyst ( substance that lowers activation energy)

  • Enzymes


    macromolecules

    speed up reactions by lowering activation energy

    specific to substrates

    do not alter chem reaction

    are not altered in reaction

    "induced fit" mechanism

  • Proton donors


    acids

    Hydrogen ion have one lone proton in nucleus

  • Hydrogen Ion receptor


    base (alkali)

  • Buffers


    keep pH in check

    consist of weak acid and corresponding anion

    major buffer in body- carbonic acid-bicarbonate ion buffer system

  • acidosis


    blood pH falls below 7.35

  • alkalosis


    loss of hydrogen ions, causes blood pH to rise above 7.45

  • salt


    any metal cation and nonmetal anion held together by ionic bonds

  • electrolytes


    salt (ionic compound) dissolve in water, resulting cations and anion in solution are electrolytes

  • hydrocarbon


    only contain hydrogen and carbon and can exist in a chain or a ring

    carbon-hydrogen backbone forms basis for all organic compounds

  • monomer


    single subunits that can combine to build larger structures

  • polymers


    many monomers linked together

  • dehydration synthesis


    2 monomers link by covalent bond to form polymers (anabolic reaction)

    products are polymer compound and molecule of water

  • hydrolisis


    molecule of water added to polymer, atoms in water molecule split, covalent bond between monomers are broken

  • monomer of carbohydrate


    monosaccharide

  • carbohydrates


    made of carbon hydrogen and oxygen

    polar and hydrophilic

    main role if fuel via catabolic and redox reactions freeing chemical energy stored in carbs, which is then used to drive synthesis of nucleotide adenosine triphosphate

  • isomer


    same molecular formula but dif structure

  • lipids


    contain carbon, hydrogen and oxygen

    non polar and hydrophobic

  • lipid monomer


    fatty acid

    hydrocarbon chain bonded to carboxylic acid

  • saturated fatty acid


    no double bond between carbons, carbons become saturated with hydrogen ions

    solid at room temp

  • monounsaturated fatty acids


    one double bond between carbons which causes chain to bend

    liquid at room temp

  • polyunsaturated fat


    two or more double bonds between carbon

    liquid at room temp

  • triglycerides


    fatty acids do not package into long chains, they are stored by linking 3 fatty acids via dehydration synthesis to a modified 3-carbon sugar called glycerol

    produces triglyceride which are stored in fat cells

  • phospholipid


    similar to triglyceride

    in place of third fatty acid we find a phosphate group (4 O and 1 P atom)

    head is polar and hydrophilic, tail is nonpolar and hydrophobic

  • steroids


    class of lipids

    4-ring hydrocarbon structure

    cholesterol forms basis for other steroids

  • protein functions


    enzymes

    structural roles

    body's defense

    cell-cell communication

    muscle contraction

    oxidized as fuel

  • monomer of protein


    amino acid

  • amino acid


    each type of protein made up of combo of 21 dif amino acids

    made of carbon, hydrogen, oxygen and nitrogen

    R group makes it unique

  • peptide


    amino acids linked by dehydration synthesis

  • peptide bond


    two amino acids joined by polar covalent bond

  • fibrous proteins


    long protein strand composed on nonpolar amino acids

  • globular proteins


    polypeptide chain assembled` into "globe" and are polar

  • first 2 levels of protein structure


    primary- amino acid sequence of its polypeptide

    secondary- folds of polypeptide structure stabilized by H bonds between amino acids (alpha helix or beta pleated sheet)

  • last 2 levels of proteins structure


    tertiary- final 3-D shape assumed, stabilized by H bonds, covalent bonds. Interactions between R groups. ( nearly the same to secondary )

    quaternary- manner in which polypeptide chains assemble (each chain has its own 1-3 structure tho)

  • Protein denatruation


    process that destroys proteins shape

    • heat

    • pH changes

    • chemicals

  • monomers of genetic code


    nucleotides

    nucleic acids (genetic code polymers) are not oxidized into fuel but nucleotides play a key role in energy systems (Nucleotide adenosine triphosphate)

  • nucletoide structure


    nitrogenous base

    5-carbon (pentose) sugar

    phosphate group

  • ATP synthesis


    synthesized by adding 3rd phosphate to ADP

    • highly endergonic due to neg charge in phosphate groups

  • polymers of nucleotides


    nucleic acid

    linked by dehydration synthesis