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58 Cards in this Set

  • Front
  • Back
Chemical Bonds
Covalent, Ionic, Hydrogen
Atomic particles
Protons(+) and Neutrons (no charge) found in nucleus, electrons(-)
Covalent bonds
share a pair of electrons between 2 atoms
more stable bonds
nonpolar covalent
electrons shared equally
polar covalent
one atom is more electronegativily charged which causes the electron to move closer to one atom - so one side of molecule is more positive and one more negative
Ionic bonds
2 or more ions bonded together due to their opposite charge
NaCl sodium(+) cloride(-)
Ions
an atom whose # of electrons differs from its # of protons.
when an atom gains or loses electrons.
Hydrogen bonding
linkage of an already covalently bonded H atom w an electronegative atom.
Normally a linkage that nearly always pairs H w/ O or N.
Carbon
Life based on Carbon
4 valance electrons
links w/ 4 more electrons to be stable
Covalent bonds
straight chains
Ring structures
4 atoms that make up living things
Carbon
Hydrogen
Oxygen
Nitrogen
4 Molecules of life
Carbs - CH2O - proportion
Lipids - fats
Proteins - amino acids, peptide bonds
Nucleic acids
Building blocks *
monomers - smaller building blocks that link together to create large molecules
polymers- large chains of monomers
polysaccharide - many monosaccharides units together
Carbs *
monosaccharides - glucose
disaccharides - succrose, lactose
polysaccharides - starch glycogen, cellulose, chitin
Components of carbs
Carbon
Hydrogen 2
Oxygen
carbs are stored as ________
used as ___________
glycogen
glucose
Lipids made of
Carbon. hydrogen, oxygen
lipids - long definition
pure lipids are not readily broken down.
very high energy source
stored in triglyceride form
Used in fatty acid and glycerol form
glycerol
fatty acid
types of lipids
glycerides
steroids
phospholipids
Glycerides made of 2 parts *
glycerol-specific kind of alcohol, makes head of molecule, contain OH group
fatty acid (long chain of carbon and Hydrogen atoms) w/ carboxyl group (COOH)
Triglycerides
3 fatty acids linked w a glycerol
most important of the glycerides
90% of lipid weight in foods
normally known as "fats"
Types of fat
saturated fatty acid - no double bonds
mono-unsaturated fatty acid - 1 double bond
poly-unsaturated - multiple double bonds
saturated fatty acid & health
Linked to heart disease
great source of energy
valuable source of insulators in cold weather
need to be taken in limited amounts
increases blood cholesterol
saturated fatty acid (alkanes)
saturated w/ hydrogen atoms
no double bonds
normally solid at room temps
found in animal products
and tropical oils
Unsaturated fats (alkenes)
one or more double bonds between the carbon atoms of its hydrogen chain
Steroids
linked w 4 carbon rings (cyclic hydrocarbons)
well-known ones are cholesterol, testosterone and estrogen
cholesterol
part of outer membrane of many cells
component of bile which emulsifies fat in small intestine
precursor for testosterone & estrogen
Phospholipids
glycerol head
2 fatty attached - hydrophobic
linked to 3rd OH group is a phosphate group instead of the 3rd fatty acid as in triglycerides; outer membrane of cells largely made of phospholipids - hydrophilic
proteins
enzymes
hormones
transport
contractile
protective
structural
storage
toxins
communication
enzymes
biological catalyst
speed up or enables chemical reactions in living things
Lactase
Sucrase
Lipase
Hormones
chemical messengers which prompts physiological activity w/in and organism, both plants and animals.
Thyroxin
Estrogen
Testosterone
Amino acids - short answer
building block of proteins
polypeptides are made up of chains of amino acids
20 amino acids in nature
structure of an amino acid
amino group
central carbon
carboxyl group (COOH)
-R side chain which differentiates one amino acid from another
amino acid
each amino acid has at least 1 amine.
1 acid functional group as the name implies.
The different properties result from variations in the structures of different R groups.
The R group is often refered to as the amino acid side chain
Chaining of amino acids
carboxyl group one amino acid joins to the amino group of the next w/ the loss of the water molecule
Protein Structure *
"form follows function"
Primary structure
Secondary structure
Tertiary structure
Quaternary structure
Denature
Breakdown, unfolding or altering of shape of proteins:
-PH acid, alcohol
-Heat
Metabolism
sum of all the chemical reactions that a cell or larger organism carries out
amino acid
dhscarbo
dhs lipid
dhs protien 2
metabolic pathway
a+b then c+d then e+f ....
sequentioal set of enzymatically controlled reactions where product of one reaction serves and the substrate for the next reaction.
Activation energy
energy required to initiate chemical reaction
enzymes lower activation energy needed
active site - place in enzyme where substrate binds and is transformed
coenzyme helps catalyze substrates
Enzymes
facilitate chemical process in living things.
accelerate chemical reactions that would happen anyway.
Enable reactions because living things can wait for reactions to occur naturally
Catalysts-retain their original chemical composition
Coenzymes
accessory molecule part of the activation site of an enzyme and allows it to function.
vitamins are one type
regulation of enzymes
Amount of substance
Negative feed back - product of a process that reduces the activity.
Allosteric regulation - product of a reaction binds to the enzyme
Oxidation
loss of electrons
electrons carriers molecules that shuttle electrons down the energy hill - NAD
Reduction
Gain of electrons
3 cycles of respiration
Glycolysis
Krebs cycle
Electron transport chain
Adenosine Triphosphate
nitrogen containing molecule w/ 3 phosphate groups attached.
produced in cell by breakdown of glucose. ATP used in cell by splitting and one phosphate group removed.
Glycolysis
conversion of glucose into pyruvate w/ production of ATP
Lactic acid production
o not avail
Hyd dropped back to pyruvic acid to form lactic a
some diffuses out of cell to LV
O is present LA converted back into pyruvic acid
ETS electron transport system
accepts energy from carrier in the matrix and stores it to a form that can be used to phosphorylate ADP.
two energy carriers are known to donate to ETS - NAD & FAD
ETS - NADH binds to a
prosthetic group called FMN and is reoxidized to NAD.

NAD is recycled acting as an energy shuttle
ETS - What happens to hydrogen that comes off the NADH?
FMN gets H + 2 electrons
also picks up a proton from the matrix - passes electrons to iron-sulfer clusters and forces two protons into intermembraneous space.
Proton Gradient
built up as a result of NADH feeding electrons into ETS