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62 Cards in this Set

  • Front
  • Back
  • 3rd side (hint)
Atoms
Composed of protons, neutrons (located in nucleus), and electrons. Electrons revolve around nucleus in orbital shells
Atomic number
Number of protons in an atom; in a electrically neutral atom it is also number of electrons
Ion
atom gains of loses electrons; aquiring a net electrical charge.
Molecules
2 or more atoms linked together
Covalent bond
two atoms share a pair of electrons
Polar covalent bond
one atom attracts the bonding electrons more than the other atom of the pair
unequal sharing of electron pair, unequal charge distribution
Nonpolar covalent bond
two atoms of similar electronegativities
equal charge distribution
Molecular shape
altered within limits by the rotation of their atoms around covalent bonds
Free radicals
atoms with unpaired electron in outermost orbital
highly reactive, unstable
oxidizes other atoms
Oxidation causes free radical to gain an electron and the other atom usually becomes a new free radical
Electonegativity
power of an atom to attract electrons
Ionic bonding
charged atom
electrical attraction between 2 ions with unequal charges
unequal number of protons and electrons
Cation
ion having net positive charge
Anion
ion having net negative charge
Hydrogen bonds
form between polar molecules
resulf of (+) end being attracted to (-) end.
Weak bond
determine shape of large molecules, shape determines function and ability to interact with other molecules
Bond Strength
Covalent-share electrons-strongest
Ionic-opp attract-strong
hydrogen-(H to O or N)- weak
Hydrophobic (C to H) weakest
Free radical formation
Exposure to radiation or toxins
cause DNA damage
take antioxidants to protect
Vit C and E
Water
excellent solvent-dissolves more compounds than any other solvent
capacity to absorb, store and release heat
high specific heat
heat buffer
Adhesive-water molecules adhere to the surface
Cohesive-water molecules cling together
Solution
homogeneous mixture of 2 or more kinds of molecules, atoms or ions
Solute
dissolved substance
Solvent
substance in which the solute dissolves
Solute concentration
amount of the solute present in the unit volume of solution
g/l; moles/L or 1M solution
Like dissolves like
nonpolar solutes are soluble in nonpolar solutions
polar solutes are soluble in polar solutions
Hydorphilic
dissolve in and interact with water (ions and polar covalent molecules)
water loving
Hydrophobic
do not interact with water
poorly soluble or completely insoluble (nonpolar covalent)
water hating
Amphipathic molecules
a molecule containing polare or ionized groups at one end and nonpolar groups at the other
phospholipids
in water nonpolar regions hide inside to get away from water
Hydrolysis reaction
breaking of a chemical bond with additon of elements of water (H and OH) to the products formed
Dehydration reaction
Water removed to form covalent bond
Acid
molecules that release protons (H+) in solution
more H+=more acidic
strong acids completely ionize in solution
weak acids incompletely ionize in solution
Base
molecules that accept protons (H+) in solution or releases hydroxide ions (OH-)
pH scale
based on -log [H+]
lower the pH = more acidic
higher pH = more basic
neutral solution - pH 7.0
acidic solution - pH < 7.0
basic solution - pH > 7.0
Importance of pH
cells functino in limited range 7.35-7.45
7.8-6.8 = death
enzyme activity is affected by pH
changes can casue protein denaturation- loss of function
Buffers keep pH within normal limits
Buffers take up excess H+ or OH- to minimizes changes
Orgamic molecules
Carbon based
contain carbon and hydrogen
each carbon can covalently bond to 4 other atoms
Macromolecules
Polymers composed of smaller subunits called monomers
synthesized by dehydration reactions, broken down by hydrolysis reactions
Functional groups
group of atoms attached to an organic molecue the gives it unique chemical properties
give electrical charge, polarity or make hydrophobic or hydrophilic
Carbohydrates
simple and complex sugars
important to engery production and storage
Simple sugars
Monosaccharides (monomer)
pentoses or hexoses
glucose and fructose
Disaccharides (2 bonded monosacchirides)
lactose- milk sugar
maltose- wheat sugar
sucrose- table sugar
Polysacchrides
many monosaccharides linked together to form polymers
complex sugars
starch, glycogen= store energy
cellulose and chitin are stuctural components
Lipids
hydrogen and carbon atoms
nonpolar, hydrophobic
40% of organic matter in average body
4 subgroups
Fatty acids
triglycerides
phospholipids
steroids
Triglycerides/fats
3 fatty acid molecules + 1 glycerol
Fatty acids
2 oxygen atoms with carbon and hydrogen
Saturated fatty acid
all carbons are linked by single covalent bonds
Unsaturated fatty acide
contain one or more double bonds between carbon atoms
monounsaturated- one double bond
polyunsaturated- more than one double bond
cis Fatty acid
both hydrogens on same side of double bond
H H
I I
C = C
trans fatty acid
hydrogens are opposite sides of the double bonded carbons
H
I
-C=C-
I
H
impart stability to the food for longer storage and alters the foods flavor and consistency
Eicosanoids
altered fatty acids from arachidonic acid that regulate cell functions
Phospholipids
glycerol + 2 fatty acids + phosphate group + (nitrogen-containing group)
amphipathic
forms phospholipid bilayers of cellular membranes
Steroids
structure includes 4 interconnected rings of carbon atoms
not water soluble
cholesterol, cortisol, testosterone, estrogen
Proteins
50% of organic material in the body
composed of carbon, hydrogen, oxygen and nitrogen
Polypeptides
polymers formed from amino acids joined by peptide bonds
peptide has < 50 amino acids
Amino acids
amino group
carboxyl group
varying side chains
20 different naturally occuring Amino Acids
Glycoproteins
one or more monosaccharides covalently attached to the side chaings of specific amino acids
connective tissue
mucus
Primary protein structure
amino acids linked in a chain
sequence will determin secondary and tertiary structure as well as what type of protein you have.
shape determines frunction
Secondary structure
flexibile, can bend and rotate around bonds and assume a number of shapes
H bonds positioning determines the shape
can be coiled into alpha helix shape.
H bonds can also form between peptide bonds and chain can run parallel forming straing, extended region beta pleated sheet
tertiary Protein structure
Disulfied bonds (contain sulfur) form covalent bonds, fold around form bonds between sulfur atoms and will hold tertiary shape
3D shape- way proteins fold itself in space- maintains secondary structure
Quaternary Protein structure
2 or more polypeptides join to make one protein
diverse function- hemoglobin
Nucleic acids
responsible for the storage, expression and transmission of genetic information
determins whether one is a human or a mouse, a muscle cell or an epithelial cell
DNA
dioxyribonucleic acid (DNA)
store genetic information on chromosomes
double stranded
sugar called deoxyribose
RNA
ribonucleic acid
single stranded
converts the information in DNA into proteins
DNA
identified by nitrogenous
4 bases 2 classes
1. purine base (double ring)
-adenine
-guanine
2. pyrimidine base (single ring)
-cytosine
-thymine
2 chains are held together by 3 hydrogen bonds between purine guanine and pyrimidine cytosine (C-G)
2 hydrogen bonds between purine adenine and pyrimidine thymine (A-T)
RNA
contains uracil instead of thymine
Base bair with purine adenine and uracil (A-U) pairing
the other three bases, adenine, guanine and cytosine are the same as DNA
ATP
adenosine triphosphate
purine bases
transferes energy between nutrients and cells
break down releases energy
hydrolysis releases energy
ATP in cells
used for
production of force and movement
active transport
synthesis of organic molecules