chapter 2- chemistry Flashcards
three states of matter are liquid, solid, and WHAT
gas
electrical energy
the energy of the movement of charged particles
atomic number
determined by the number of protons it has
atomic number - atomic mass
to figure out how many neutrons a element has
isotopes
atoms that have the same atomic number but different masses
half-life
the time necessary for half a given amount of a radioisotope to decay
magnesium has an atomic # of 12, how many valence electrons
2 (12 electrons hat fills the valence shell 2-8-2
why do inert atoms not contribute to the formation of molecules?
they have full valence shells
anion
an atom with more electrons than protons
non-polar single covalent bond
type of chemical bond where two atoms share one pair of electrons equally
for hydrogen bonds to be created, there must first be molecules that
have WHAT covalent bonds between hydrogen and another atom
polar
catabolism
decomposition reactions of the body
An enzyme is a biological WHAT substance that facilitates a
reaction without becoming part of the reaction
catalyst
hydrophobic
molecules that don’t dissociate in water to create a solution
base
substance that dissociates to release cations and hydroxide ions
colloid
term for a solution that contains large molecules
A disaccharide is formed by the WHAT synthesis of two WHAT
dehydration and monosaccharides
unsaturated fatty acids
contain one or more double covalent bonds
prostaglandins are an example of lipids that are derived from arachidonic
acid and belong to the WHAT group of lipids
eicosanoid
glycolipid
a diglyceride with a carbohydrate group
steriods
the lipid group that is based on the carbon ring structures
due to the bipolar nature of phospholipids, they will spontaneously adopt a
WHAT structure, with the heads pointing out and the tails pointing in, when placed in water
micelle
peptide bond
covalent bonding between the amino group of one amino acid and the carboxyl group of another form
R group amino acids
have a common core structure, but they differ from each other
the local folding and twisting that occurs because of H-bonding between nearby
amino acids form the helices and sheets of the WHAT structure of a protein
secondary
native conformation
protein in its proper shape
excessive heat or the wrong pH can WHAT a protein
denature
active site
where the enzyme has the specificity to bind to its substrate
cofactor
ion or molecule that binds to an enzyme to activate it
glycoprotein
molecule that consists of a small part carbohydrate and a large part protein
nucleotide nitrogenous base that is found in RNA but not DNA
uracil
WHAT serves as the copy of DNA instructions for creating the primary structure of a protein
messenger RNA/mRNA
ATP(adenosine triposphate)
two extra phosphate groups attached to an A base nucleotide for RNA form the high energy molecule
organic molecules
-carbon-based molecules with hydrogen(minimum) and oxygen
-produced by living things
-allows the formation of large molecules with other molecules
-either solid or solutions
carbon skeleton
chain of carbon with hydrogen
macromolecules
-small organic molecules
-involves dehydration synthesis of monomers into polymers
polymers
linkages of multiple monomers
solution
uniform mixture
colloid
containing dispersed proteins or other large solutes
suspension
solution containing large particles that settle(ex:blood)
carbohydrates
-3% of body
-starches and sugar
-catabolized for energy
-building blocks for DNA, RNA, amino acids and nutrient reserves
monosacchride
-simple sugar(glucose)
-made of C6H1206
-fructose
isomers
two molecules have same chemical formula but differ in shape
disacchride
-sucrose(glucose + fructose)
-two covalently bonded monosaccharides
-created by dehydration synthesis
-catabolized by hydrogen
polysaccharide
-3 or more monosaccharides
-storage form of glucose produced by skeletal muscle and liver cells
lipids
-12-24%
-fats, oils, waxes, nonpolar
-energy storage for longer, cell membranes & cellular communication
fatty acids
-hydrocarbon chain with carboxyl groups
-hydrophobic making molecule insoluble
functional groups
bonding of carbon and hydrogen with other elements
saturated and unsaturated fatty acids
-one or more double covalent bond
-saturated= animal source(unhealthy)
-unsaturated= plant source(healthy)
leukotrienes
signal injury in cell communication
prostaglandins
pain and inflammation after injury(coordinates events)
glycerides
-C3H8O3 + fatty acids
-number of fatty acids bonded to glycerol group by dehydration
a.monoglycerides
b.diglycerides
c.triglycerides
-make up fat deposits on animals
-energy storage
-insulation
-mechanical protection(knees and eye sockets)
organic molecules(excess of them)
can be converted into triglycerides for storage via dehydration synthesis
steriods
-ex: cholesterol, estrogen, & testosterone
-important for cell membrane formation & maintenance
-cell division and osmotic stability of cell
-tissue metabolism & mineral balance
-regulation of sexual function
-processing of dietary fats
phospholipids
-diglyceride + phosphate(non-lipid)
-predominant of cell membrane
glycolipids
diglyceride + carbohydrate
micelle
sphere formed with hydrophilic heads oriented out toward the water and
hydrophobic tails pointed away from water
proteins
-20% of body mass
-essential to cell structure and function
-from amino acids that become polypeptides that are folded into proper native conformation
a.support
b.movement
c.transport
d.buffering
e.coordination & control
f.defense
g.metabolic activity and regulation
amino acid structure
-central carbon
-carboxyl groups
-amino acid groups
-R group
-20 different amino acids
-some charged
-some hydrophilic
-some hydrophobic
-some make disulfide bonds
* resulting bond = peptide bond
polypetide
chain of peptide-bonded amino acids
primary structure
unique sequence of amino acids directed by DNA
* dictated by genes within DNA
secondary structure
local twisting/folding of polypeptides between neighbor amino and carboxyl groups to H
tertiary structure
global folding due to chemical interactions between R groups
quaternary structure
aggregation of 2 more or more tertiary-folded polypeptide chains (for multi-subunit proteins)
globular
compact, rounded, soluble
fibrous
sheets or strands, non-
soluble
enzymes
-abundant protein in the body
-biological catalyst, catalytic protein used metabolism of living cells
-speed up reactions by lowering activation energy, orient molecules to favor reaction without heat or pressure
enzyme specificity
unique 3D shape creates a pocket called an active site
enzyme saturation limit
maximum rate of reaction, adding more substrate will increase the reaction rate until saturation
substrate
a molecule that an enzyme reacts with
enzyme saturation
active site full and reaction can go no faster to produce products
enzyme regulation
co-factors can turn enzymes on and off and provides short term control over reaction
coenzymes
non-protein organic molecules that acts as co-factor
anabolic reaction
building of molecules
conjugated proteins
bound to other organic molecules
glycoproteins
small carbohydrate attached to large protein
ex: mucus
proteoglycan
large polysaccharide linked by polypeptides
ex: “glue” in connective tissue
nucleic acids
-less than 1% of body mass
-stores and processes info at molecular level
-composed of nucleotides
- 2 types: DNA & RNA
nucleotides
-linked by dehydration synthesis
-3 parts:
1. pentose sugar(ribose or deoxyribose)
2. phosphate group
3. nitrogen bases
nitrogen purine base
-double ring
-adenine & guanine(A,G)
nitrogen pyrimidine base
-single ring
-cytosine, thymine & uracil (C,T,U)
linear “backbone”
sugar of one nucleotide to
phosphate of next creating a line with the bases hanging off the side
RNA (ribonucleic acid)
-protein synthesis
-single-stranded
-backbone = ribose & phosphate
- bases: A,U,G,C
- 3 types:
1.mRNA
2.rRNA
3.tRNA
mRNA (messenger)
template for a protein, order of amino acids (the primary structure of a protein)
rRNA (ribosomal)
forms ribosomes: organelle for protein synthesis
tRNA (transfer)
carrier to bring amino acids to ribosomes
DNA (deoxyribonucleic acid)
-double helix
-contains genes
-backbone = alternating deoxyribose sugar & phosphate
-order of nucleotides in DNA is the info. copied into mRNA form so it can assemble the primary structure of a protein
-bases: A,T,C,G
gene
specific order of one strand of DNA that encodes RNA visually encodes a protein
high energy molecules
-used to hold chemical bond energy from food molecules in an easy-to-use form
-involves phosphorylation
-phosphate groups negative charge
-when cell has extra energy, phosphate is bonded to ADP(low energy form) to store energy as ATP(high energy form)
phosphorylation
bonding of phosphate group to an organic molecule
ATP (adenosine triphosphate)
-adenine + ribose + 3 phosphates
-hydrolysis of a bond to 3rd phosphate releases energy
