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Phys Ch 2

exam 1 material

QuestionAnswer
medical imaging depends on ... behavior of atoms and molecules
CT scan external radiation
PET scan looking at radiation already present in the body (internal radiation)
MRI no radiation, just magnetic field and sound waves (H+ electron shift)
atoms are made up of... protons, neutrons, and electrons
atomic number the number of protons
atomic weight the number of protons and neutrons
atoms that make up >99% of atoms in the human body hydrogen, oxygen, carbon, nitrogen
elements that make up 0.7% of atoms in the human body mineral elements, like calcium, potassium, phosphorus, sodium
if electron's outermost shell doesn't have a full 8 electrons is chemically reactive
most abundant form of carbon 12C
the radioactive carbon isotope 14C
what determines osmolarity? atoms
one mole of any element... contains the same number of atoms (6.022 x 10^23)
anions negative
cations positive
if an atom loses or gains electrons.. it becomes an ion
what atoms readily form ions? hydrogen atoms and most mineral atoms
ionic form of mineral elements electrolyte
molecule two or more atoms bonded together
strongest bond covalent bond
free radical unpaired outer shell of electrons, highly chemically reactive
example of free radical free oxygen or hydroxide mlx
what does a free radical do to the body? leads to DNA damage, cancer, lose ability to control cell cycle
substances dissolved in a liquid solute
liquid in which solutes are dissolved in solvent
solutes dissolved in a solvent to form... solution
what molecules dissolve in water? ionic/polar mlx (covalent DO NOT)
osmolarity of human blood 300 mosMoles
osmolarity of sodium in human blood 140 mEq/L
osmolarity of chlorine in human blood 100 mEq/L
osmolarity of potassium in human blood 4.5 mmol/L
where does the rest of the osmolarity come from in human blood? dissolved proteins
mmol the number of particles
mEq the number of particles AND electrical charge
amphipathic molecules has hydrophilic and hydrophobic end, when mixed with water forms clusters
amphipathic mlx function provides maximal interaction between water and polar ends, acts as emulsification agents
emulsification agent can bind to lipid mlx and make them soluble in water (polar)
acids increase concentration of H+ in a solution
bases decrease the concentration of H+ in a solution
pH amount of H+ in a solution
human pH range 7.35-7.45
primary reason we have to maintain a tight pH range.. all proteins in the body function in a very narrow pH range
4 types of organic mlx in human body carbohydrates, lipids, proteins, nucleic acids
polysaccharides more than 3 monosaccharides
lipids make up of hydrogen and carbon atoms, linked by non polar covalent bonds
4 subclasses of lipids fatty acids, triglycerides, phospholipids, steroids
cortisol, aldosterone, testosterone, estradiol, are all made from... cholesterol
cortisol most powerful catabolic mlx in the human body
testosterone most powerful anabolic mlx in the human body
proteins of all living organisms are composed of the same set of _____ amino acids, with ____ different side chains 20,20
how many essential amino acids are there? 9
essential amino acids body can't make them, but must eat them in our diet
how many nonessential amino acids are there? 11
nonessential amino acids body can produce them on their own
all amino acids have... a carboxyl group and an amino group, just different side chains
primary protein structure sequence of amino acids written out in order
secondary protein structure protein starts to fold up on itself
why does a protein start to fold up on itself? because of chemical interactions between charges on side chains on other molecules, and the cell environment (Water)
2 primary structures of secondary alpha helix and beta pleated sheet
tertiary protein structure interactions fold polypeptide into its final 3D shape, water affects folding
the final 3D shape of a protein conformation
all proteins have _____, only some have _____ all Proteins have primary, secondary, tertiary, only some have quaternary
quaternary protein structure individual polypeptides start to come together, shape of final quaternary structure is different from function of individual polypeptides that make it up
example of quaternary protein structure hemoglobin
Created by: thomask9
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