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Exam 1, Ch. 1, 2, and 3

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  • Energy


    the capacity to do work or put matter into motion . Greater the work the more energy

    Can be transformed from potential to kinetic energy, stored energy can be released, resulting in action

  • Kinetic Energy


    energy in action

  • Potential Energy


    stored (inactive) energy

  • 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

  • Protons


    carry positive charge, weigh an arbitrary 1 atomic mass unit

  • Neutrons


    Have No charge or neutral charge , weighs 1 atomic mass unit

  • Electrons


    carry a negative charge, are so tiny they virtually have no weight (0 atomic mass unit)

  • Atomic mass unit


    AMU

  • Ionic bond


    complete transfer of valence electrons from one atom to another .

    Opposite charges attract (cations + anions)

    Example. Salts like sodium chloride

  • Covalent bond


    sharing of valence electrons between two atoms.

    Sharing more electron pairs create stronger bond

    (Single= 2electrons, Double= 4electrons, Triple= 6electons)

    Polar and nonpolar

  • Hydrogen bond


    weak attraction between a positive hydrogen atom and an electronegative atom on another molecule

    Not A true bond (acts like a weak magnetic attraction )

    Gives liquid water its properties and holds large molecules in 3D shapes

  • Anion vs Cation


    negatively charger ion (gained electron) Vs positively charged ion (lost electron)

  • Nonpolar covalent bond


    equal sharing of electrons between atoms

    Charge balanced/ no charge

    Example. Carbon dioxide

  • Polar covalent bond


    unequal sharing of electrons between atoms

    Charge partially negative, and partially positive, ends dipole.

    Example. Water

  • Primary structure of Protein


    linear sequence of amino acids forming a polypeptide chain

  • Secondary structure of protein


    primary chain coils into spirals ( a-helices) or folds into sheets (B-sheets)

    Held together by hydrogen bonds

  • Tertiary structure of protein


    a-helices and B-sheets fold up to form a compact 3D globular molecule

    Held together by intramolecular bonds

  • Quaternary structure of protein


    two or more polypeptide chain (subunits) combine to form a functional protein

  • 4 levels of protein structure


    primary, secondary, tertiary, quaternary

  • Introns


    non-coding regions that are removed/filtered out before translation

    Filler

  • Exons


    coding regions that are expressed (spliced together to form final mRNA)

  • Transcription


    DNA - mRNA

    Occurs in nucleus: copies genetic code

  • Translation


    mRNA-protein

    Occurs in cytoplasm/ribosome: builds amino acid chain using mRNA, tRNA, and rRNA

  • Passive transport


    No ATP required: moves substances down concentration gradient (high to low)

    Examples, simple diffusion, facilitated diffusion, osmosis

  • active transport


    requires ATP; moves substances against concentration gradient ( low to high) or uses vesicles

    Example, Na+ / K+ pump, endocytosis, exocytosis

  • Homeostasis


    The body’s ability to maintain a stable relatively constant internal environment despite continuous external changes

    Receptors (monitors stimulus) control center (process info ) and effector (Carries out response/feedback)