1/334
Looks like no tags are added yet.
Name | Mastery | Learn | Test | Matching | Spaced |
---|
No study sessions yet.
anatomy
describes the structures of the body and how the parts fit together
physiology
describes the function of the body parts and how they work
structure
structure of a body part affects its function
function
function of a body part affects its structure mechanically or chemically → informs and shape the structure
Levels of Organization - smallest to largest
Chemical level → cellular level → tissue level → organ level → system level → organismal level
Homeostasis
condition of equilibrium through regulation and feedback adjusting to get to healthy system normal - most homeostatic controls are negative feedback
2 systems that regulate homeostasis
Nervous system → sends nerve impulses - fast and specific
Endocrine system → sends hormones - slower and broader
Receptor
detects changes and sends signal to control centre
control centre
determines set point and creates a response to an effector
effector
carries out appropriate response to get back to equilibrium to either reduce or amplify stimulus
negative feedback
the response reduces/stops the stimulus preventing severe change within the body → back to normal healthy (set point)
response
decreases the difference between the current level and set point
positive feedback
the response enhances or magnifies the stimulus, and amplifies its effect - controls events that do not require continuous adjustment
homeostatic imbalance
occurs when the control centre cant respond properly to stimulus. leads to dysfunction and disease
anatomical position
human standing, feet apart, palms forward, thumbs away from body
axial division
head and torso
appendicular division
limbs - arms and legs
sagittal section
divides body into left and right
frontal section
divides the body into front and back
transverse section
divides the body into top and bottom
dorsal body cavity
contains cranial cavity and vertebral cavity
ventral body cavity
contains thoracic cavity and abdominopelvic cavity
parietal serosa
lines body cavities
visceral serosa
lines organs
matter
mass and occupies space
energy
puts matter into motion
potential energy
stored energy
elements of human body - macromolecules
oxygen 65%, carbon 18%, hydrogen 10%, nitrogen, 3% - make up 96% human body mass
lesser elements comprise
2.6% body mass
trace elements comprise
<0.4%
Calcium
adds hardness to bones and teeth - essential for nerve and muscle function
Magnesium
helps muscle and nerve functions and bone health. maintains blood glucose levels and helps absorbs nutrientsp
Phosphorus
essential for DNA and RNA and for making ATP
Sodium and Potassium
produced electrical activity in neurons and muscle cells
sulfur
used to make amino acids for building proteins
iron
used to carry oxygen in our RBC
zinc
helps replicate DNA, produce more immune cells
Iodine
regulates metabolism
elements are defined by
atomic number and atomic massi
isotopes
atoms that have a diff number of neutrons than normal for that element
anion
gains electrons and is negative charge
cation
loses electrons and is positive charge
molecules
2 or more atoms together
molecule
two or more different elements
mixture
made of different types of molecules
synthesis reaction
2 components combined to make a larger more complex molecule - anabolic building activity
decomposition reaction
bonds are broken between components of a larger molecule - catabolic bondbreaking activity
exchange reaction
bonds are broken and formed to rearrange the components of the reactants - involves both synthesis and decomposition
reduction-oxidation reaction
reduced when gain electrons
oxidized when lose electrons
LEO GER
glucose oxidized oxygen reduced
increases rate of chem rxns
temperature, concentration of reactants, particle size
catalysts
increase rate of rxn without being chemically changed or becoming part of product. - ie enzyme
biochemistry
the study of chemical composition and rxns of living matter
inorganic compounds
does not contain carbon
organic compounds
large compounds that contain carbon
water
most abundant inorganic compound 60-80% volume of living cellswa
water properties
high heat capacity - stabilize temp
high heat of vaporization - helps w cooling
reactivity - hydrolysis and dehydration synth.
cushion and lubrication
water dissolves
ionic and polar substances
dehydration synthesis
covalent bond is created by removing OH from one molecule and H from another releasing H2O
hydrolysis
covalent bond is broken by adding OH from water to one molecule and H to the other
ions are also
electrolytes because it conducts electrical currents in a solution
acids
proton donors - releases hydrogen ions H+
bases
proton acceptors - absorbs H+ in solution releases OH-
neutralization reaction
occurs when acids and bases are mixed together - displacement rxn occurs and forms water and a salt
buffers
resists large changes can act like a weak acid or weak base
bicarbonate buffer
maintains blood pH
monosaccharides
single sugar units made of 3-7 carbons
disaccharides
formed by dehydration synthesis of 2 monosaccharides
polysaccharides
large chains of monosaccharides joined together by dehydration synthesis
starch
used for glucose storage in plant cells
glycogen
used for glucose storage in animal cells - in liver to help blood sugar levels
cellululose
made of glucose but most animals do not have enzymes to hydrolyze it
triglycerides
stores energy, insulates, and protects
phospholipids
used in cell membranes - made up of a glycerol and 2 fatty acids plus a phosphate group
steroids
signalling molecules like hormones
saturated fatty acids
all carbons linked via single covalent bonds - solid at room temp.
unsaturated fatty acids
one or more carbons are linked by double bonds so it’s not saturated with hydrogen atoms. liquids at room temp
prostaglandins (an eicosanoid)
regulates blood pressure and inflammation increases pain receptors and induces fever
nonsteroidal anti-inflammatory drug NSAID
inhibits prostagladins to decrease pain, inflammation, and fever. ie asprin and ibuprofen
proteins
amino acids held together with covalent bonds
peptide bond
amine group and acidic carboxyl group
all human proteins
20 diff types of amino acids → one amine group and carboxyl groups plus 20 diff R side chains
r group side chains
give each amino acid its characteristics → size, polarity, and pH
primary structure
order of amino acids in the polypeptide chain → hard to break peptide bonds need an enzyme to break it
secondary structure
refers to shapes like alpha helices and beta pleated sheets that form w/ amino acids from the primary structure interact w/ each other through hydrogen bonds
tertiary structure
the three-dimensional shape of a single polypeptide chain. shape comes from how chain folds, based on regions of amino acids that are hydrophilic or hydrophobic or disulphide bridges
quarternary structure
occurs when 2 or more polypeptide chains join tgt to make one functional protein multimer - not all proteins have quartnerary structure
fibrous proteins
rope-like insoluable molecules that are hard to break
globular proteins
compact spherical, water soluable, chemically active molecules that oversee cellular functions. ie. enzyme, protein, antibodies, hormones
protein denaturation
loss of the specific 3-D structure of a globular protein leading to loss of function. done by either change in pH or temperature
enzymes
lower activation energy for a chemical reaction and increases rate of rxn without needed high temperatures
enzyme consist of
apoenzyme (protein portion) and cofactors (metal ions) or coenzymes(organic molecules)
holoenzymes
apoenzymes together with necessary cofactors or coenzymes
enzyme substrate complex
enzyme and substrate together at an active site - catalyzes rxn and turns substrate into products
DNA nucleotides
has a deoxyribose sugar nitrogen base and a phosphate group
purines
adenine and guanine
pyrimidines
cytosine and thymine
purine pairs with pyrimidine by
hydrogen bonding
base pairing
A-T and G-C
DNA and RNA strands are
synthesized from 5’ to 3’
RNA is used
to take nucleotide sequence info from DNA and use to make proteins