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7 chemical groups most important in biological processes
1. hydroxyl group
2. carbonyl group
3. carboxyl group
4. amino group
5. sulfhydryl group
6. phosphate group
7. methyl group
cabonyl group
(=C=O)
compound name: ketone aldehyde
ex. acetone
# of molecules in a sample measured in
moles
water freely dissociates into
- hydrogen ion (H+): the hydrogren atom leaves it's electron behind
-hydroxide ion (OH-): the molecule that has lost the hydrogen ion
-hydronium ion (H30+): the moleculre that gained the hydrogen ion (H+)
what determines ph
changes in the relative concentration sof hydroxide and hydronium (amount of H+)
Acids
- substance that INCREASES the H+ concentration of a solution
- HCl --> H+ CL- (dissociates in liquid water, more H+ in water)
- ph values LESS than 7
Bases
- substance that REDUCES the H+ concentration of a solution
- NaOH --> Na+ + OH-
- Basic solutions have Ph GREATER than 7
Ph scale
- concentration of H+ and OH- are equal in pure water
- adding acids or bases modifies these concentrations
- ph is used to describe if a substance is acidic or basic
buffers
- weak acids or bases that can react with strong acids or bases to prevent sharp, sudden changes in pH
- minimize changes in concentrations of H+ and OH-
- combine reversibly
ex. ammonia
three classes of macromolecules that are polymers
1. carbohydrates
monomer: glucose
2. proteins
monomer: amino acids
3. nucleic acids
monomer: nucleotide
hydroxyl group
(-OH)
compound name: alcohol
ex: ethanol
carboxyl group
(-COOH)
compound name: carboxylic acid or organic acid
ex. acetic acid
Amino Group
(-NH2)
compound name: amine
ex. glycine
sulfhydryl group
(-SH)
compound name: thiol
ex. cysteine
phosphate group
(-OPO3^-2)
compound name: organic phosphate
ex. glycerol phosphate
methyl group
(-CH3)
compound name: methylated compound
ex. 5-Methyl citosine
gene expression
The process by which information encoded in DNA directs the synthesis of proteins or, in some cases, RNAs that are not translated into proteins and instead function as RNAs.
molecular mass
The sum of the masses of all the atoms in a molecule
Molarity
the number of moles of solute per liter of solution
Avagadro's number
6.02 x 10^23, the number of atoms or molecules in 1 mol
Polymer
A long molecule consisting of many similar or identical monomers linked together.
monomer
small chemical unit that makes up a polymer
Four macromolecules
carbohydrates, lipids, proteins, nucleic acids
enzymes
specialized macromolecules that speed up chemical reactions
dehydration reaction
when two monomers bond together through the loss of a water molecule
hydrolysis
process by which polymers are dissasembled into monomers, the reverse of the dehydration reaction
natural polymers
rubber, starch, protein, and DNA
synthetic polymers
man made polymers
nylon, polyester, teflon, epoxy
simplest carbohydrates
Monosaccharides or simple sugars
Carbohydrate macromolecules
polysaccharides, polymers composed of many sugar building blocks
monosaccharides molecular formula
usually multiples of CH2O
(1C:2H:1O)
How are monosaccharides classified?
The location of the carbonyl group (as aldose or ketose)
The number of carbons in the carbon skeleton
Disaccharide
formed when a dehydration reaction joins two monosaccharides
glycosidic linkage
A covalent bond formed between two monosaccharides by a dehydration reaction.
The architecture and function of a polysaccharide are determined by
its sugar monomers and the positions of the glycosidic linkages
starch
A storage polysaccharide in plants consisting entirely of glucose monomers
simplest form of starch
amylose
how do plants store starch?
in granules called plastids which include chloroplasts
glycogen
storage polysaccharide in animals
where is glycogen mainly stored?
liver and muscle cells
hydrolysis of glycogen
releases glucose when the demand for sugar increases
cellulose
A substance (made of sugars) that is common in the cell walls of many organisms
the most abundant polymer
can cellulose be broken down to formulate ATP?
no, with the exception of bacteria in cows stomach or termites gut bacteria
cellulose vs starch
different glycosidic linkages:
- alpha (α) ring form
- beta (β) ring form
they are isomers of each other but their difference defines their availability to be used
Chitin
Polysaccharide found in arthropod exoskeletons and fungal cell walls.
Lipids are not polymers (true or false)
true
unifying feature of lipids
hydrophobic (not soluble in water)
most biologically important lipids
fats, phospholipids, steroids
fats (tryglycerides) building block molecules
glycerol and fatty acids
Glycerol
A three-carbon alcohol to which fatty acids are covalently bonded to make fats and oils.
fatty acids
carboxyl group attached to a long carbon skeleton
Fats separate from water because
water molecules form hydrogen bonds with each other and exclude the fats (they are NOT repellant of each other)
ester linkage
three fatty acids joined to glycerol
triacylglycerol
A lipid consisting of three fatty acids linked to one glycerol molecule
fatty acids vary in
length (number of carbons) and in the number and locations of double bonds
saturated fatty acids
have the maximum number of hydrogen atoms possible and no double bonds
- solid at room temp b/c shape is linear so molecules can be packed closer together
unsaturated fatty acids
A fatty acid possessing one or more double bonds between the carbons in the hydrocarbon tail. Such bonding reduces the number of hydrogen atoms attached to the carbon skeleton.
- liquid at room temp b/c shape is bent and non linear, more space and less dense
trans fats are a subtype of:
unsaturated fat
Mono-unsaturated Fats
have one double bond
Poly-unsaturated Fats
have many double bonds
Hydrogenenation
the process of converting unsaturated fates to saturated fats by adding hydrogen -- creates trans fats
major function of tryglecerides
energy storage in animals
adipose cells
cells that store fat
adipose tissue
cushions vital organs and insulates the body
white adipose tissue
white fat, in which excess calories are stored in the body
- more white adipose as you age
- less mitochondria
- purpose: resoivar of fat molecules in times of food scarcity
brown adipose
- metabolizes fats so you can produce ATP
- more in babies
why are seeds and nuts full of fats?
- starch is a long time energy storage carb molecule in plants
- sometimes seeds need to be fueled by a more energy dense molecule -- tryglicerides
amphipathic molecule
one side hydrophillic, one side hydrophobic
phospholipids:
a lipid consisting of a glycerol bound to two fatty acids and a phosphate group.
Steroids
lipids characterized by a carbon skeleton consisting of four fused rings
Cholesterol
a type of fat, is a component in animal cell membranes and a precursor from which other steroids are synthesized
Enzymatic Proteins
Function: Selective acceleration of chemical reactions
Example: Digestive enzymes catalyze the hydrolysis of bonds in food molecules
defense proteins
Function: Protection against disease
Example: Antibodies inactivate and help destroy viruses and bacteria.
storage proteins:
Function: Storage of amino acids
Examples: Casein, the protein of milk, is the major source of amino acids for baby mammals. Plants have storage proteins in their seeds. Ovalbumin is the protein of egg white, used as an amino acid source for the developing embryo.
transport proteins
Function: Transport of substances
Examples: Hemoglobin, the iron-containing
protein of vertebrate blood, transports
oxygen from the lungs to other parts of the
body. Other proteins transport molecules
across membranes, as shown here.
hormonal proteins
Function: Coordination of an organism's
activities
Example: Insulin, a hormone secreted by the
pancreas, causes other tissues to take up
glucose, thus regulating blood sugar,
concentration.
recpetor proteins
function: response of cell to chemical stimuli
ex. the receptors built into the membrane of a serve cell detect signaling molecules released by other nerve cells
contractile and motor proteins
Function: Movement
Examples: Motor proteins are responsible
for the undulations of cilia and flagella.
Actin and myosin proteins are responsible
for the contraction of muscles.
structural proteins
Function: Support
Examples: Keratin is the protein of hair,
horns, feathers, and other skin
appendages. Insects and spiders use silk
fibers to make their cocoons and webs,
respectively. Collagen and elastin proteins
provide a fibrous framework in animal
connective tissues.
different groups of amino acids
- hydrophobic R-groups linearly arranged (non-polar)
- polar side chains; hydrophilic
- electrically charged side chains; hydrophillic
- acidic (negative charge)
- basic (positivly charged)
peptide bond
The chemical bond that forms between the carboxyl group of one amino acid and the amino group of another amino acid
primary structure of proteins
sequence of amino acids
secondary structure of protein
the coils and folds result from hydrogen bonds between repeating constituents (amino and carboxyl groups) of polypeptide
alpha α helix
beta β pleated sheet
no r group interactions
Terciary structure of a protein
: the overall shape of a polypeptide results from interactions between R groups (hydrogen bonds, ionic bonds, hydrophobic interactions, and van der waals interactions)
- disulfide bridges: strong covalent bonds that reinforce structure
tertiary structure can change if chemical environments is changed b/c structure is never fixed.
disulfide bridges
covalent bonds that may further reinforce the shape of a protein
Van Der Waals attraction
Weak noncovalent interaction, due to fluctuating electrical charges, that comes into play between two atoms within a short distance (DISTANCE DEPENDANT) of each other.
-collectivly van der waals interactions can be strong -- but not individually
ex. gecko's toe hairs and wall surface
Quaternary Structure
- result of two or more polypeptide chains bound together to form one macromolecule
- not always present in proteins
ex. hemoglobin, collegen (abundant in mammals)
Structure = function example (sickle cell anemia)
sickle cell = singular change in primary structure (one amino acid difference) that has cascading effects and creates misshapen red blood cell
Factors affecting protein structure
primary structure but ALSO physical and chemical conditions:
- alterations in Ph, salt concentration, temperature, or other environmental factors can cause protein to unravel
denaturation
loss of a protein's native structure
(ex. frying an egg changes the temperature of the environment
- proteins in egg white provide viscosity in the aqueous solution
- frying pulls apart the proteins from the evaporating water
- linearization of protein creates closely packed together = solid egg white)
cells fold proteins in several stages (true or false)
true
Diseases associated with misfolded proteins
Alzheimer's, Parkinson's, and mad cow disease
Enzymes
proteins that act as catalysts to speed up chemical reactions
- can perform their functions repeatedly, functioning as workhorses that carry out the processes of life
- even a single mistake in its primary structure can have a domino effect on all other orders of structure
The process/cycle of enzymatic activity
1. substrate enters the active site; the enzyme changes shape such that the active site enfolds the substrate
2. substrate held in the active site by weak interactions such as hydrogen bonds and ionic bonds
3. the active site lowers the activation energy and speeds up the reaction
4. substrates are converted to products
5. products are released
6. active site is available for two new substrate molecules
What determines the amino acid sequence of a protein?
genes
Gene
sequence of DNA that codes for a protein and thus determines a trait
DNA
a nucleic acid made of monomers of nucleotides
nucleotides
the building blocks of nucleic acids consisting of a five-carbon sugar, a nitrogenous base, and a phosphate group.
DNA provides directions for its own replication (true or false)
true
How does DNA control protein synthesis?
DNA directs synthesis of messenger RNA (mRNA) and, through mRNA, controls protein synthesis