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hydrocarbons
molecules consisting only of carbon and hydrogen
functional groups
specific groups of atoms attached to carbon backbones (C-C)
types of functional groups
Hydroxyl, carbonyl, carboxyl, amino, sulfhydryl, phosphate, methyl
isomers
organic molecules having the some molecular or empirical formula can exist in different forms
structural isomers
where the differences are in the actual structure of their carbon skeleton
stereoicomers
have the same carbon skeleton but differ in how the groups attached to this skeleton are arranged in space.
macromolecules
extremely large molecules, consisting of polymers of similar smaller molecules (monomers) linked by covalent bonds
monomers
when ____ are covalently linked together, they form a polymer
polymers
a long molecule built by linking together a large number of small, similar chemical subunits called momomers
carbohydrates
starch, glycogen, cellulose, chitin
nucleic acids
DNA, RNA
proteins
functional, structures
lipids
fats, phospholipids, prostaglandins, steroids, terpenes
starch and slycogen
subunit: glucose
function: energy storage
example: potatoes
cellulose
subunit: glucose
function: structural support in plant cell walls
Example: paper or strings of celery
chitin
subunit: modified glucose
function: structural support
DNA
subunit: nucleotides
function: encodes genes
RNA
subunit: nucleotides
function: needed for gene expression
functional
subunit: amino acids
function: catalysis and transport
example: hemoglobin
structural
subunit: amino acids
function: support
example: hair and silk
fats
subunit: glycerol and three fatty acids
function: energy storage
example: butter and corn oil and soap
phospholipids
subunit: glycerol, two fatty acids, phosphate, and polar R groups
function: cell membranes
example: prostidylcholine
prostaglandins
subunit: five-carbon rings with two nonpolar tails
function: chemical messengers
example: prostagladin E (PGE)
steroids
subunit: four fused carbon rings
function: membrtanes and hormones
example: cholesterol and estrogen
terpenes
subunit: long carbon chains
function: pigments and structural support
example: carotene and rubber
dehydration synthesis
removes OH and H during synthesis of a new molecule. this is how monomers form polymers.
hydrolysis
breaks a covalent bond by adding OH and H. This is how polymers can also be broken back down into monomers
protein functions
enzyme cataysis, defense, transport, support, motion, regulation, storage
enzyme catalysis
facilitates chemical reaction
defense
that recognize foreign cells
transport
transports small molecule and ions
support
form the matrix of skin, tendons, etc.
motion
by sliding or contracting allow movement inside the cells
regulation
hormones that are intercellular regulations
storage
Ca++ and iron are stored by binding to proteins
proteins
are polymers of amino acids
peptide bonds
a protein is composed of one or more long chains of amino acids linked by ______
polypeptidtes
these are the chains that hold the protein together
nonpolar and nonaromatic
Alanine (Ala), valine (val), isoleucine (ile), leucine (leu), glycine (gly)
nonpolar and aromatic
phenylalanine (phe)
tryptophan (trp)
nonpolar and special function
proline (pro)
methionine (met)
polar uncharged and nonaromatic
serine (ser)
threonine (the)
asparagine (asn)
glutamine (gln)
polar uncharged and aromatic
tyrosine (tyr)
polar uncharged and special function
cysteine (cys)
charged and nonaromatic
glutamic acid (glu)
aspartic acid (asp)
distidine (his)
lysine (lys)
arginine (arg)
shape
protein function is determined by its _____
primary
specific amino acid sequence
secondary
folding of amino acid chains primary due to H--H
motifs
folds or creases (super secondary structure)
foiling and coiling
due to interactions among R groups and surrounding water
Interactions between R groups
Hydrogen bonds
Di- sulfide bridges
ionic bonds
van der waal's forces
hydrophobic exclusion
tertiary
final folded shape of globular protein (3-D)
domains
functional units coded by an exon
quaternary
forms when two or more polypeptide chains (subunits) associate to form a functional protein.
domains
functional units within a larger structure
Chaperone proteins
help other proteins to fold correctly
monosaccharides
the simplest of the carbohydrates
dissaccharide
two monosaccharides linked together
polyaccharides
are longer plyners made up of monosaccharides that have been joined through dehydration reactions
starch
a storage polysaccharide, consists entirely of alpha-glucose molecules linked in long chains
cellulose
a structural polysaccharide, also cosists of beta- glucose molecules linked in chains
glysogen
the comparable molecule to startch in animals
chitin
the structural material found in arthropods and many fungi
RNA
ribonucleic acid
nucleic acid
a chain of five-carbon sugars linked together b phosphodiester bonds with nitrogenous base protruding from each sugar
adenosine triphosphate
the energy currency of the cell
amino acids
contain an amino group and an acidic carboxyl group
helix
peptides that are coiled into a spiral
beta sheet
a secondary structure can occur between regions of peptide aligned next to each other to form a planar structure
tertiaty structure
the final folded shape of a globular protein
denaturation
if a proteins environment is altered, the protein may change its shape or even unfold completely
dissociation
for quartnary structure, that may be dissociated without losing their individual tertiary structure
lipids
a somewhat loosely defined group of moecules with one main chemical characteristic. they are insoluble in water.