Exam One - 1.2 Biochemistry 101 Flashcards
What are the primary elements of life?
CHON
Which CHON element is the human body most abundant in?
Hydrogen
Which CHON element is the earth most abundant in?
Oxygen
Which CHON element is not in everything?
Nitrogen
Molar solution
one mole of substance/ one liter of solution
isotope
same element, different weight
ion
same element, different charge
atomic number
how many protons in an element
atomic weight
protons + neutrons
cations
positively charged
lost electrons
anions
negatively charged
gained electrons
What are the four major biological roles of electrons?
1 - covalent bonds (share)
2 - ions: opposites attract
3 - high-energy electrons: electrons with excess captured energy
4 - free radicals: unpaired electrons, can damage other biological molecules
ionic bond
gains or loses an electron, but does not share
opposite charges attract
functional groups
combo of elements that frequently occur in biological molecules
move between molecules as a single unit
hydrogen bond
weak bond
H must bind with a N,O, or F
cause of water surface tension
van der waals forces
weak and nonspecific
results from temporary formations of dipoles
hydrophilic
like water (have dipole moments)
hydrophobic
scared of water
lipids have no dipole moments
solute
any substance that dissolves in a liquid
solvent
the liquid in which a solute dissolves
what is the universal solvent?
water
solution
combination of solutes dissolved in water
Concentration = ?
solute amount/volume of solution
What are the building blocks of the cell?
sugar
fatty acids
amino acids
nucleotides
what are the larger units of the cell?
polysaccharides
fats/lipids/membranes
proteins
nucleic acids
What are the three types of carbs?
monosaccharide
disaccharide
polysaccharide
What are the two kinds of monosaccharides?
five-carbon sugar
six-carbon sugar
What are the two five-carbon sugars?
ribose and deoxyribose
What are the three kinds of sex-carbon sugars?
fructose glucose and galactose
What are three kinds of disaccharides?
sucrose maltose and lactose
What makes up sucrose?
glucose and fructose
What makes up maltose?
glucose and glucose
What makes up lactose?
glucose and galactose
What polysaccharide do humans use?
glycogen
What are different kinds of lipids?
saturated fatty acids
monounsaturated fatty acids
polyunsaturated fatty acids
cholesterol
steroids
membranes
What are fats?
fatty acids linked with a glycerol
What are the basic components of a phospholipid?
choline and phosphate and glycerol make the hydrophilic head
one saturated and one unsaturated lipid chain makes the hydrophobic tail
What are the nucleotides for RNA?
uracil and cytosine
adenine and guanine
What are the nucleotides for DNA
thymine and cytosine
adenine and guanine
What are the three basic components to make a nucleotide?
nitrogenous base
five carbon sugar
one phosphate
What are the two purines?
adenine and guanine
What are the three pyramidines?
cytosine, thymine, and uracil
What is the product of transcription?
mRNA
What is the product of translation?
Proteins
What is the basic building block of proteins?
Amino acids
What is the difference between essential and non-essential amino acids?
essential AA you must get from your diet, the body can manufacture non-essential AA
What are the four levels of protein structure?
primary: AA peptide chain
secondary: alpha helix or beta sheets due to hydrogen bonding
tertiary: three dimensional folding
quaternary: more than one peptide chain
What are polymers?
biomolecules made of repeating units
What is an example of a polymer?
glycogen is a polymer of glucose
True or False? Protein-binding reactions are reversible
True
Affinity
degree to which a protein is attached to a ligand
Equilibrium
the rate of binding is exactly equal to the rate of unbinding
Agonist
competing ligands that mimic each others actions
Antagonist
competing ligand that blocks the action of another
proteolytic activation
protein does not function correctly until peptide fragments are removed
Cofactor activation
must have a cofactor bind to an inactive protein to make it active (so the ligand can then attach)
Allosteric activator
binds to inactive protein on opposite side of the binding site in order to change protein shape and make it active
Competitive inhibition
binds to site so that the true ligand cannot and makes protein inactive
allosteric inhibition
binds to active protein on opposite side of the binding site in order to change protein shape and make it inactive again
What are some factors that could affect protein binding?
temperature, pH, amount of protein in cells, reaction rate
When is the maximum reaction rate reached?
When the protein is saturated
