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100 Terms
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capillary action
the process by which a plant takes up water against gravity without energy
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cohesion
water forming hydrogen bonds with water molecules
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adhesion
water forming hydrogen bonds with other substances ex. water on glass
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hydrophilic
attracted to water (polar)
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hydrophobic
not attracted to water (nonpolar)
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hydrocarbons
chains consisting of only carbon & hydrogen
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trace elements
required by an organism, but only in minute qualities
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isotopes
forms of an element with different numbers of neutrons
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radioactive isotopes
used in medicine for diagnosis and treatment
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chemical bonds
interactions between valence electrons of different atoms
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nonpolar covalent bond
electrons are shared equally
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Electronegativity
tendency to attract electrons in a covalent bond
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polar covalent bond
one atom has more electronegativity, so unequal sharing forms areas of partial + and - charges
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ionic bonds
bonds from attraction between oppositely charged ions
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hydrogen bonds
weak bonds between +H of H2O and -O or N of another molecule, play a role in 3D shape of proteins and nucleic acids
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van der waals interactions
weak connections because of uneven distribution of electrons, contribute to 3D shape
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transpiration
movement of water molecules up thin xylem tubes and their evaporation from the stomata in plants, the H20 clings to each other by cohesion & to the walls by adhesion
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specific heat
amount of heat required to raise/lower the temperature of a substance by 1 degree Celcius
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solvent
dissolving the solute
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solute
being dissolved by the solvent
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solution
the solvent and the solute together
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acids
excess H+ ions H+ > OH-
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bases
excess OH- ions OH- > H+
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pure water
pH of 7, H+ = OH-
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buffers
substances that minimize changes in pH, accept H+ ions when hydrogen molecules are in excess & give H+ ions when hydrogen molecules are depleted, essential in living tissues (ex. blood)
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carbonic acid (H2CO3)
buffer that moderates pH changes in blood plasma & the ocean
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major elements in life
C, H, O, N, S, and P: carbon, hydrogen, oxygen, nitrogen, sulfur, and phosphorus
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organic compounds
contain C, most have H
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carbon
forms large, complex, and diverse molecules, 4 valence electrons, forms up to 4 covalent bonds (single, double, or triple)
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isomers
molecules that have the same formula but differ in arrangement, results in molecules that differ in biological activities
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What do the properties of an organic molecule depend on?
depends on the carbon skeleton arrangement and the functional groups attached to it
alcohols like ethanol & methanol, they help dissolve molecules like sugars
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carboxyl group function
carboxylic acids like fatty acids & sugars, they have acidic properties because it tends to ionize, source of H+ ions
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carbonyl group function
ketones like aldehydes such as sugars
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amino group function
amines such as amino acids
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phosphate group function
organic phosphates, like ATP, DNA, and phospholipids
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sulfhydryl group function
in the amino acid cysteine, makes disulfide bridges in proteins to stabilize their structure, compounds end in -thoil
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methyl group function
doesn't increase solubility, when it binds to DNA it can affect gene expression
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polymers
long chain molecules made of repeating subunits called monomers ex. starch, a polymer made of glucose monomers ex. proteins, polymers made of amino acid monomers
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What bond is stronger, covalent or ionic bonds?
covalent bonds are stronger
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hydrolysis
when water is added to split large molecules, the reverse reaction of dehydration
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dehydration synthesis
creating polymers from monomers, 2 monomers are joined by removing 1 molecule of water, requires energy & enzymes
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carbohydrates
simple sugars (glucose, fructose, galactose) & polymers (starch) made from these & others subunits, all carbs exist in a ration of 1 carbon : 2 hydrogen : 1 oxygen ration (CH2O)
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monosaccharides
the monomers of carbohydrates ex. glucose and ribose
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polysaccharides
polymers of monosaccharides ex. starch, cellulose, glycogen
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What happens when you change the structure of a molecule?
it changes the function
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starch
glucose monomers with 1-4 alpha linkages that the body can digest
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cellulose
glucose monomers with 1-4 beta linkages that the body can't digest
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polysaccharide function
energy storage and structural support
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starch function
storage polysaccharide found in plants ex. potatoes
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glycogen function
storage polysaccharide found in animals (vertebrate muscle cells & liver cells)
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cellulose function
major component of plant cell walls
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chitin
in exoskeleton of arthropods (lobsters & insects) & cell walls of fungi
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lipids
hydrophobic molecules not made of polymers ex. wax, oil, fat, steroids
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fats (triglycerides)
made of a glycerol molecule and 3 fatty acid molecules
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fatty acids
hydrocarbon chains, nonpolar & hydrophobic, a long hydrocarbon tail with a COOH group @ the head
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saturated fatty acids
no double bond between carbons, tendons to pack solid @ room temp, linked to heart disease, produced by animals ex. butter, lard
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unsaturated fatty acids
have some double carbon bonds that result in kinks, liquid @ room temp, made by plants ex. corn, olive oil
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lipid function
energy storage, they hold 2x the calories per gram as carbs & protection and insulation, in mammals it's stored in adipose cells
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phospholipids
make up cell membranes, have a hydrophilic (polar) head that includes a phosphate group, have 2 fatty acid tails that are hydrophobic
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How are phospholipids arranged?
they are arranged in a bilayer that form the cell membrane, they have hydrophilic heads that point toward the cytosol/extracellular environment & the hydrophobic tails are in between
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steroids
made of 4 rings that are fused together
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cholesterol
a steroid that is a common component of cell membranes
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estrogen and testosterone
steroid sex hormones
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amino acids
central carbon bonded to a carboxyl group (COOH), an amino group (NH2), a hydrogen atom, and an R group (a variable group/side chain)
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primary protein structure
unique sequence in which amino acids are joined
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secondary protein structure
1 of the 2 3D shapes resulting from hydrogen bonding between members of the polypeptide backbone
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alpha helix
coiled shape of protein
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beta pleated sheet
accordion shape of protein
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tertiary protein structure
complex globular shape resulting from interactions between side chains (ex. hydrophobic interactiosn, van der waals, hydrogen bonds, disulfide bridges)
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How are globular proteins (ex. enzymes) held in position?
they're held in position by R group interactions
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quaternary protein structure
the association of 2 or more polypeptide chains into 1 large protein
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hemoglobin
globular protein w/quaternary structure because it's composed of 4 polypeptide chains
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What disease stems from an abnormal hemoglobin resulting from a single amino acid substitution of valine in the 6th spot?
sickle cell disease
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Denaturation
when a protein loses its 3D shape, due to pH, temp, or salt, and it loses it's biological function
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What is the simplest hydrocarbon?
methane
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characteristics of methane
nonpolar, not soluble in water, hydrophobic, stable, little attraction between molecules, gas at room temp
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How can hydrocarbons grow?
by adding C-C bonds
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geometric isomers
molecules that differ in arrangement around a C=C bond, but have same covalent partnerships
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enentiomer (stereo) isomers
molecules that are mirror images of each other, left-handed and right-handed versions
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thalidomide
one version of the molecule gives birth defects and one gets rid of morning sickness
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functional group definition
components of organic molecules that are involved in chemical reactions
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aldelhyde
if a C=O bond is at the end
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ketone
if a C=O bond is in the middle
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macromolecules
smaller organic molecules join together to form larger molecules
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sugars
end in -ose & are classified by the number of carbons