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