10.1
what does a nonpolar amino acid look like?
all have hydrocarbons in some way
identify where the N-terminus, C temrinus and peptide is on a bond
N-terminus is at the left
C-terminus is at the right
peptide bond is in the middle
define protein denaturization
the keeping of the primary structure
keeping primary structure in tact
identify active site and substrate
active site- the location of the reaction (location of enzyme)
substrate- reactant (starting material)
polar amino acids?
hydrogen and oxygen bonds at the end
what the the levels of protein structure?
Tprimary(1)- order of amino acids
secondary (2)-localized regular structure backbone (alzhiemers)
tertiary(3)- overall 3d structure (single chain) determined by 1 degree t sidechains
quaternary (4)- same as tertiary but between subunits
list the causes of protein denaturation
heat above 50 C (cooking food)
acids, bases, ionic compounds (lactic acid from bacteria, denaturing milk)
reducing agents (thiols)(used for perms and relaxers)
detergents (membrane proteins)
heavy metal ions (mercury and lead poisoning)
mechanical agitation (whipped cream, meringue)
distinguish cofactor, coenzyme prosthetic group
cofactor- metal cation: Mg2+, Zn2+
coenzyme- organic not a metal, vitamins
prostehtic group- subgroup of coenzymes
what do polar amino acids have diff. compared to acidic amino acids?
polar neutral amino acids have NH2 where acidic polar amino acids have double and single bonds of oxygen
the level of attractive forces of protein structures
primary- helps with the overal strcture
secondary- helps with formation by hydrogen bonds and an amino acid
tertiary- a single chain attracted to aqueous surroundings
quartery- same as tertiary
what are the attractive forces affected for..
heat above 50 C
acids, bases, ionic compounds
reducing agents
detergents
heavy metal ions
mechanical agitation
hydrogen bonds, hydrophobic interactions
salt bridges, hydrogen bonds
disulfide bonds
hydrophobic interactions
sal bridges
hydrogen bonds, london forces
what is lock and key model, and induced fit model of ES
lock and key- active site, exact complementary, very substrate-specific
induced fit model- flexible and can change in active site
polar basic amino acids
basic´s have long chains
identify functions of proteins
hormone
receptors
transporter
hormone- messenger
receptors- outside can trigger
transporter- channel carrier
factors with low activation energy
substrate concentration(needs to be a steady state)
changes in pH
temp
inhibitors
drugs
explain pKa and pH information on unprotonated and protonated
the determination of the isoelectic point within the titration curve