week 1 (intro to chem, proteins/carbohydrates, body cavities) Flashcards
atom
A nucleus containing protons and neutrons, surrounded by a shell of orbiting electrons
(neutral)
valance electrons
of electrons on the outermost shell
why are valance electrons important
atoms are most stable when their valence shell is full
covalent bond
each atoms unpaired electron are SHARED by both nucli to fill their orbits
Ionic bonds
electrons are TRANSFERED between one atom to another
Non polar colvent bonds
electrons shared evenly between two atoms
bond is symmetrical
polar covalent bonds
electrons are shared unevenly
Electronegitive atoms
These atoms like to “hog” electrons (which in turn can create non polar covalent bonds)
examples of electronegtivie atoms
nitrogen
oxygen
clorine
positive electrolytes
cation
negative electrolytes
anion
Water
universal solvent
like dissolves like which means polar solvent(water) dissolves polar molucules
6 unique properties of water
Liquid water is an excellent solvent cohension adhension water is denser as a liquid than as a solid water has a high specific heat water has a high heat of vapourization
liquid water is an excellent solvent why?
it is stable
both ‘negitive’ and ‘positive’ sides
charged molecules love water
cohension
similar things attatrched together
binding between molcules
surface tension
adhension
attraction between two different particles
H20 denser as a liquid than solid
ice is less dense than water so it floats on itself
ice is more volumious/uniform shape than water
specific heat
amount of energy required to raise a temp of 1g of a sibstance by 1C. (how easy it si to increase the kinetic energy in a system)
calories
energy needed to do something
4.13
how much enegery is needed to change 1 mil of water by 1C
4.13J
or a calorie
heat of vapourization
the energy required to change 1g of a substance from liquid to gas
endothermic reactions
absorb/require heat to proceed
also known as anabolic or synthesis reactions
Gibbes free energy change ^G > 0 or a positive ^G (endergonic)
dehydration
exothermic reactions
release heat
also known as catabolic or decomp
GFEC ^G < 0 or a negitive ^G (exergonic)
energy
the capacity to do work or supply heat
potential energy
stored energy
kinetic energy
energy of movement
first law of thermodynamics
energy is conserved, it can not be destroyed on created
entropy
amount of disorder
spoutunous events favour disorder (exothermic)
entropy always increases (disorder increases)
disorder is opposite of energy it is the loss of it
what makes a reaction spontanous
products have lower potential energy and higher entropy than the reactants
products less ordered and more disordered than reactants
breaking bonds
hydrocarbons
carbon chain
amino function group
look for nitrogen
tend to attract protons
have NH2 group (can act as a base and pick up hydrogen which makes it a postivie charge)
carboxyl group
look for OH
tend to donate protons
hydrophllic
carbonyl group
type of carbon chain hydrophillic serve to link two large carbon containing molucules ketones have R groups aldehydes have hydrogen
hydroxyl group
very electronegitive due to O
very polar and high solubitly (if oxygen is present in a molcule always expect polarity)
has O-H group
no carbon
phosphate group
phospolipid
acts as a means of transfering eneegry from one molcule too another
one end can be very polar which can create a hydrophobic end
contain PO4
ATP (transfers chemical energy between organic molecules during chemical reactions)
sulfhydryl group
can form disufide bond which is important to protien structure
very polar due to electronegitive of S
form disiphlfide bridges
secondary stucture
curly hair people have more of these groups
has S-H group
dissulfhydryl group
has two s instead of one
non - ionized amino acid
chiral carbon (carbon with four different things attached)
an amino group and a carboyl group (both neutral)
not an ion
ionized amino acid
amino group more postive and carboxyl group more negitive (whole structure neutral)
will deprotien in a basic solution (pH will depend on how will behave)
the importantance of charges in amino acids
if their charged they’re more likely to assoiate with water
make them more liekly to react with other compounds
hoe soluble a amino acid is depends on the pH of the solution they’re in
amino acid types
r group responsible for what the amino acid does
look for electronegative R groups (soluble with water, oxygen)
look for giving off proteins (negative charges) acidic
look for gaining proteins (postive charges) basic
polymer
repeating subnits
hydrolysis
water breaking bonds
primary protein structures
linear amino acids
secondary protein structures
2D structure created by interactions between amino acids
hydrogen bonding/electrostatic interactions
NOT a protein yet, a polypedtide
tertiary protein sturctures
3D structures created by interactions of R groups in amino acids of that polypemtide chain
happens due to hydrophoblic/hydrophillic interaction
depends on the pH of the enironment
about 4 apart
quanterany protein structures
assembly of multipke protiens into a function unit (liccute in salt)
2 or more polypedtide held together
protein folding
often spontantous
because of hydrogen bonds and van der Waals interactions make folded molecule more stable than unfolden
denatured protein
unfolded protein that is not able to function normally
shape in altered
not destroyed, covlent bonds/peptides can be renatured(put in different enironment)
catalyst
speed up the rate of reaction (enzymes)
3 factors of rxns
concentratin
temp
angle of collision
reactant molecules bind to the active site
when the substrates binds to the enzyme’s activatino site, the enzyme changes shape slightly. This “induced fit” results in tigher binding of the substrates in the active site
electrostatics in moloecule binding
substrateas with electrostatic impressions can alter shape of enzyme
enzyme with electrostatic interaction can flex/change substrates
Three steps of enzyme action
initiation
transition state facilitation
termination
initiation process
reactants bind to the active site in a specific orientations, forming a enzyme-substrate complex
combining of both creates shape change which generates products
‘squeezed fit’
trnsition state facilitation
interactions between enzyme and substrate lower the activiation energy required induced fit (squeezed)
termination process
products have lower affinity for active site and are released. enzyme is unchanged after the reaction
competitive inhibition
occurs when a moolecule similar in size and shape to a substrate competes with it for the active site binding
allosteric regulation
occurs when a molecule casues a chnage in enzyme shapae by bindning to the enzyme at a location other than the active site
cofactors of enzymes
coezymes
factors apoenzymes need to become holozyme
can be organic(minerals) and inorganic(vitamins)
holoezymes vs apoenzymes
holoezymes are whole enzymes while apoanzymes need a coemzyme to function
regions of body
head(skull/face) neck(supports head/attachs trunk) trunk(chest,adomen,pelvic) upper limbs(arms/shoulder) lower limb(butt/legs)
superior direct
towards head
inferior direct
away from head
aneterior direct
near front
posterior direct
near back
medial direct
near midline (left and right line)
lateral direct
futher from midline
intermediate direct
between two structures
contralateral direct
opposite side as structure
ipsililiateral direct
same side as structure
proximal direct
nearer to attachment of limb to trunk or orgin of structure
distal direct
futher to attachment of limb to trunk or orgin of structure
superfical direct
on surface
deep direct
internal
sagittal plane
vertical plane
midsagittal plane
equal vertical split of body/organ
parasagittal plane
unequal vertical split of body/organ
midline
equal vertical split of body
frontal plane
split from back and front
transverse plane
split horizontally
oblique plane
split at an angle
cranial cavity
formed by cranial bones, contains brain
vertebral cavity
formed by vertebral column, contains spinal cord and beginning of spinal nerves
thoracic cavity
chest
contains pleural, pericardical cavities and ediastinium
pleural cavity
potential space between the layers of pleura that surrond the lungs
pericardial cavity
potential space between the layer of pericardium that surrond the heart
mediastinum cavity
central portioin of thoracic cavity, contains heart, thymus, espophus, trachea, several large blood vessels
abdominopelvic cavity
subdivided into the abdomin and pelvic cavity
abdominal cavity
contains stomach, spleen, liver, gallbladder, small intentine, most of larger intestine, derous membrane of the cavity is peritoneum
pelvic cavity
contains urinary bladder, some of large intestine and reproductive organs
what are all the cavities
cranial, vertebral, thoracic, plural, pericardical, mediastinium, abdominiopelvic, abdominal, pelvic
epithelial tissue
covers bosy surfaces, lines hallow organs, cavities and ducts. also forms glands. allows body to interact with internal/extental enironments
connective tissue
protects/supports the bosy and it’s organ types bind organs together, store energy from fat, help provide body with immunity from disease
muscular tissue
cells specialized for contraction and generation of force, in the process generates heat for the body
nervous tissue
detects change in varity of conditions and respsonses by generating electeral signals call nerve action protenation
different types of tissue
epithelial, connective, muscular, nervous
major elements of body
oxygen, hydrogen, nitrogen and carbon
less elements of body
calcium, phosphous, sulfur, sodium, chlorine, megnesium and iron
element
pure substance
nucleus
contains protons n neutrons
proton
carry charge (+)
electron
carry charges (-) orbit the nucleus
atomic number
number of protons
how do valance charges form chemical bonds
atom is most stable when valence shells are filled this is through chemical bonding
whats the nature of hydrogen bond
The hydrogen bond is an attractive interaction between a hydrogen atom from a molecule or a molecular fragment X–H in which X is more electronegative than H, and an atom or a group of atoms in the same or a different molecule, in which there is evidence of bond formation
surface tension
surface tension happens when the combined effects of cohension and adhenison happens. this creates a meniscus
properties of carbon (how they make it useful to formation of larger molecules
it is useful because it has four valance electrons
this always it to form many covlent bonds
organic compounds relating to carbon
carbon is basically the foundation of organic compounds because of the 4 valance electrons in the outermost shell
carbon skeleton
The term carbon skeleton is used to describe the pattern in which the carbon atoms are bonded together in a molecule
hydrocarbon
hydrocarbon is an organic compound consisting entirely of hydrogen and carbon
functional groupds relating to carbon
functional groups attach to carbon
functional groups have a specific arrangement of atoms
monomer
Monomers are small molecules, mostly organic, that can join with other similar molecules to form very large molecules, or polymers
monosaccharide
momers that are used to build carbohydrates
end is “ose” with the prefix of how many carbons coming first
disaccharides carbohydrates
consists of two monosaccharides that have combined by dehydration synthesis
simple sugar carbohydrates
monosaccharide and disaccharides are simple sugar carbohydrates
polysaccharides carbohydrates
contains tens or hundreds of monosaccharide molecules joined through dehydration synthesis.
not soluble in water
glycogen polysaccharides
a type of polysaccharide and main polysaccharide in the body.
starch polysaccharides
polysaccarides that are formed by glucose in plants
in foods such as pasta
cellulose polysaccharides
polysaccharides form from glucose by plants that cannot be digested human
protein
A protein is a naturally occurring, extremely complex substance that consists of amino acid residues joined by peptide bonds
protien structural
form structural framework for various parts of the body
hair, kertain in skin, fingernails
protein regulatory
function as hormones that regulate various physiological processes horomone insulin
protein contractile
allow shortening of muscule cekks, which produces movements
mysosin, actin
protein immunolgical
aid responses that protect the body against foregin substances and invading pathogen
protein transport
carry vitual substances throughout the body
hemoglobin
conformational change
The theory of induced fit predicts that enzymes undergo conformational changes as they bind their substrate
enzyme
in living cells calayasts are protein molecules call enzymes
three compents of enzymes
- enzymes are highly specific (each enzyme only binds with specific substrates)
- enzymes are efficient (can speed up reactions because they are an organic catalyst
- enzyme are subject to cellular controls (rate of synthesis and their concentration are dependant on the cells gene)
organism
An organism is an individual form of life that is capable of growing and reproducing, and have one or more cells
organ
Organ is the name we give to functional elements in the body and quite often they are also physically distinct such as your kidneys, your liver, your heart. Those are all defined by a shape and a location in your body and they are also defined by a function
organ systen
An organ system is a group of organs that work together to perform one or more functions
tissue
Tissue is a group of cells that have similar structure and that function together as a unit.
cell
he smallest unit that can live on its own and that makes up all living organisms and the tissues of the body
organelle
organelles are specialized structures that perform various jobs inside cells
moleule
a group of atoms bonded together
cephalic
head
cervical
neck
brachial
arm
forearm
antebrachial
thigh
femoral
leg
crural
armpit
axillary
inguinal
groin
list the four quardates of the abdomonopelvic
left, right upper quadrant
left, right lower quadrant
vertical split (median line) horizontal split (transumbilical line)
nine abdomonopelvic region
row 1
right, left hypochondraic region
epigastic region
row 2
right,left lumbar region
umbilical region
row 3
right,left inguinal region
hypogastric region
4 lines for nine regions
vertical
right,left midclavicular lines
horizontal (top) - subcostal line
horizontal (bottom) - transtubercular line
