BIOL 434 Exam 1

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1.List the four non-covalent interactions encountered in living systems

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1.List the four non-covalent interactions encountered in living systems

van der waals forces, hydrophobic interactions, hydrogen bonding, and dipole-dipole forces

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1.Explain the general characteristics of non-covalent interactions and the significance of such interactions in biological systems

solvents impact their strength, they have a cumulative effect that is highest in the native state, they decrease the free energy of the system while releasing binding energy

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1.Describe the origin of hydrogen bonds and give examples of molecules that form hydrogen bonds

N,O,S are attracted to H through partial charge differences

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1.Recognize the characteristics of hydrogen bonds and the importance of hydrogen bonds

water drives the movement of electrons across the membrane and interacts with amino acids through H bonding to drive molecular action- h bonds are stronger w/o water

they also form in between hydroxyl, carbonyl groups, and form between nucleotides

when the hydrogen acceptor is in a straight line with the H, the bond is stronger

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1.Explain what ionic interactions are and how they form

they are an attraction or repulsion of pos/neg charges, us. btwn Ca2+, phospho, carboxyl, amino groups

water stabilizes them by creating h-bonds around them which decreases the hydrostatic attraction around them

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1.Explain what is meant by the hydrophobic effect, how hydrophobic interactions occur, and their importance

includes the exclusion of polar bonds from a non-polar solution as non-p regions cluster to decrease the SA that interacts with the aq sol’n

water forms a highly ordered cage around to decrease the number of h bonds while the bulk phase around is less ordered

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1.Define amphipathic molecule and explain what happens when such molecules are placed into water

partially hydrophobic/philic. will curl into a micelle to increase entrophy, philic is exposed and phobic is in the center

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1.Explain what Van der Waals forces are

all molecules do this as attractants and repulsions due to internal charges

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Describe what weak acids and bases are

do not dissolve completely in sol’n

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Explain what is meant by a conjugate acid-base pair and give examples of such pairs

acid donates a H making the conj base

acetic acid becomes acetate

carbonic acid becomes bicarbonate

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Give examples of monoprotic, diprotic, and triprotic weak acids


acetic acid, pyruvic acid, lactic acid


carbonic acid, succinic acid


phosphoric acid, citric, glutamic

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Give the equation for the dissociation (ionization) constant, Ka

Ka= [A-][H+]/[HA]

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Describe what Ka is a measure of and how Ka is used to determine pKa

Ka tells how easily an acid loses a proton, where a higher Ka indicates a stronger acid

pH= pKa + log ([A-]/[HA])

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Explain what the pKa value of a weak acid indicates

a lower pKa indicates a stronger acid

when pKa = pH, half of the acid has dissolved in sol’n so it is half acid half base

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Predict the predominant molecular species present in a solution containing a weak acid

at: pKa1- the carboxyl group is de protonated,

pKa2- amino group is deprotonated, pKa3- R group is ionized

as the pH increases, acids lose more protons

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Describe what titration is and the information that a titration curve provides us

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Explain what a buffer is

it is a sol’n made of an acid and its conjugate base that has a capacity of +/- 1 of the pKa

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explain the importance and examples of buffers in biological systems, and consequences of malfunctions in buffering

phosphate and bicarbonate buffers are found in humans

carbonate becomes bicarbonate where carbonic anhydrase allows for Co2 to form which diffuses from capillaries to the lungs as CO2

when you exhale you release CO2 from the lungs which lowers the amount in the capillaries so equilibrium shifts to make more CO2 and hyperventilation occurs so kidneys reabsorb more CO2 into the blood

too much acid= acidosis, occurs from too much met byproduct, and too little= alkalosis from hyperventilation due to HCl leaking from the stomach or respiratory blockage

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Describe how buffers work

conj acid and base each donate or accept new protons to avoid drastic pH changes

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Recognize the mathematical relationships between pH, pKa, and buffer concentration defined by the Henderson-Hasselbalch equation

pH=pKa + log([A-]/[HA])

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Solve various problems to determine pKa, pH, molar ratios, concentrations of compounds, and volumes to mix using the Henderson-Hasselbalch relationship

see hw sheet

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Recognize and describe the structure of amino acids (AA) and recognize the different ways AAs are depicted


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2. Describe AA stereochemistry, the types of stereoisomers, and how D and L forms of AAs are determined

can be in L or D form (compared to Ala) amino group is on the left (left is more common) L and D are enantiomers

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3. Classify each of the 20 AAs commonly found in proteins into categories based on their R-groups

non-polar non-aromatic:

gly, ala, val, met, leu, pro, ile

(usually inside of the protein bc hydrophobic, gly is flexible)


trp, phe, try

polar uncharged:

ser, thr, cys, asn, gln

(csy makes disulfide bonds to stabilize 2o structure can form H bonds)

pos charge:

lys, arg, his

(not all pos at pH 7, arg can become guanidium, his has an imidazole ring, ionic interactions)

neg charge:

glu, asp

(ionic interactions and carboxyl makes it neg)

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4. Recognize and draw each of the 20 AAs commonly found in proteins as well as the AAs citrulline and ornithine


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5. Give the three letter and the single letter abbreviation for each of the 20 AAs commonly found in proteins


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6. Recognize that many more than 20 amino acids exist and some common AA residues in protein are modified post synthesis although some are introduced during protein synthesis


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Recognize selected modified AAs found in proteins and list in which proteins specific uncommon AAs are found

4-hydroxyproline and 5-hydroxylysine = collagen

6-N-methyllysine = myosin

gamma-carboxyglutamate = prothrombin

desmosine = elastin

selenocysteine = mod during synth from a UGA stop codon mod with own tRNA

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8. Recognize selected AAs that undergo reversible modification

phosphoserine, photyrosine, phosphothreonine

omega-n-methylarginine, 6-n-acetyllysine, glutamate y-methyl ester, adenylytyrosone

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  1. List AAs that are not found in protein but nonetheless have important biological functions

ornithine and citrulline are synthetic part of the urea cycle

thyroxine is a polytyrosine:

iodine + tyrosine with enzyme thyroperoxidase makes thyroglobin, monoidenotyrosenase and di, add I to T’s to make T3 and T4

glutamate is decarboxylated to GABA

his is decarboxylated to histamine

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10. Explain why AAs have ionic properties and utilize the terms amphoteric and zwitterion to describe AAs

they have a pos and neg end that can change as the pH of the sol’n changes as AA are amphoteric. When at the pI point, the AA is a zwitterion or pos and neg at the same time but electrically neutral

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11. Describe the general ionization patterns of AAs, sketch the titration curve for various AAs, and identify/label points on the curve such as where all species are fully protonated or deprotonated, the isoelectric point (pI), where the AA is a zwitterion, inflection points

screaming check the ppt

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12. Define peptides, draw a simple peptide when given the name of the peptide, and name the peptide when it is already drawn out


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Recognize that peptides can ionize and predict the overall charge of a short peptide at a given pH


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14. List peptides of physiological interest and what role those peptides play

lamosine= alanly serine dipeptide

enkephalins= pentapeptides that bind like opiates to receptors

oxytocin= nonapeptide that forms a disulfide bond and cyclic structure

antibiotics w/ 2 chains, gramicidin s and tyrocidine A are a cyclic mixture of D and L

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List the four levels of protein structure

primary secondary tertiary quaternary

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2. Explain what is meant by conformation and native state of a protein

conform is rotation around a cov/ peptide bond and the native state maximizes the non-covalent interactions and lowers the free E

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3. Explain why only one or a very few possible conformations exist for protein under typical biological conditions

only a few can be thermodynamically the most stable due to the decrease in free E

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4. Describe the ways that conformation is stabilized

non-cov interactions, disulfide bonds (intracellular environment isn’t good for making DSB)

max weak interactions is the most stable and lowers free E

hydrophobic interactions do the most to stabilize proteins bc they result in the most increase in entropy of the universe, polar charged aa have to be balanced by aa of opposite charge, water doesn’t interfere with internal environment

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5. Define what is meant by 1°structure, why knowing 1°structure is useful, and how 1°structure is a determinant of conformation

is AA sequence, used to tell mech of action of a protein for disease pathology, evolution, ect

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6. Describe what is meant by polymorphism

2 similar forms of same AA sequence (like HbA and HbS of hemoglobin) dift tissues might have different forms and shouldn’t dicrease function

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7. Describe the peptide bond backbone and the various bonds and bond angles involved

peptide bond is planar and backbone is planar in trans configuration bc of pos and neg charges

R groups would clash if cis (pro has some cis)

are specific bond angles for dift types

N-alpha and Calpha- C can rotate but C-N don’t rotate (peptide bond)

impact secondary structure

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8. Define what is meant by 2°structure

the local spacial arrangement for main chain atoms (not R group)

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what are the three major types of 2°structure

a-helix, b-conformation/b-pleated sheet, b-turn

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what are the specific characteristics of alpha-helix

r groups protrude outside of the helix

bp are 1.5A apart and 3.6 res to make 1 helix

are elastic

form between the H bonds of amide and the O of the carbonyl group

(L amino and D aa make up the helix and if added separately will disrupt structure)

are us right handed (amino end points right)

some amino acids are more likely to form a helix

(aa that decrease change in delta G are more likely to form a helix) bc charged R-groups might repel or be too big and disrupt structure (can’t have 2+ adjacent)

amino term is pos carboxyl is neg

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what are specific char of beta sheets

made of 2-12 strands (us 6aa per strand)

polypep bb extends into a zig zag

3.5A btwn aa (larger gap than alpha h)

R groups are on opposite sides

2+ strands are linked via H bonds based on parallel or anti, arrow shows the carboxyl end

bond angles change depending

anti= each aa forms 1 H bond with adjacent aa

par= each aa forms 2 h bonds with adjacent aa

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what are specific char of beta turns

polypeptide reverses direction (180degree turn) anti-prolyl connectors

4 amino acids make up each one

type 1: make up the second residue (pro) and is not flexible

type 2: third res (gly) is flexible

form middle H bonds to hold turn in place

proline cis-isomer forms the turn (bc trans is straight)

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0. Predict the 2°structure of a short sequence of amino acids

for alpha helix: amino term is pos carboxyl is neg so r-groups will oppose those charges, pro will not form alpha, gly is V flexible so will

for beta sheets: if multisheets are stacked, gly + ala are found at the surface bc they are small while large aromatic branched aa are us in the middle, pro on edges

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Define / Describe what is meant by 3°structure and how a protein would be held together

conformation of the backbone and the r-groups

alpha helix crosslinked by DS bonds, beta conformation, collagen triple helix

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2. Describe what is meant by prosthetic group, conjugated / holoprotein, metalloprotein, glycoprotein, lipoprotein

non-peptide structure required for tert structure to form

conjugated/ holoprotein have something intertwined with the protein, metallo= metal group, glyco= sugar, lipo= fat

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  1. Describe the two major groups of proteins including their characteristics and their typical functions

globular: have lots of secondary structure types like alpha and beta, us enzyme, receptor, transport protein (like hemoglobin)

fibrous: hydrophobic, noncov, long, sheets, shape support external protection function (like keratin)

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4. Describe the structural patterns of globular proteins including: a. The definition of motif and different types of motifs

b. The basic rules of folding

c. The four different structural classifications based on motif

motif= folding patterns (super secondary structure) w/ 2+ elements

beta-alpha-beta loop= can make an alpha beta barrel

beta barrel

TIM barrel= alpha outside beta strand inside

all beta= no cross-over connections seen, us. right hand,

twisted beta sheets are more stable

some are all alpha folding, some are mixed

<p>motif= folding patterns (super secondary structure) w/ 2+ elements</p><p>beta-alpha-beta loop= can make an alpha beta barrel</p><p>beta barrel</p><p>TIM barrel= alpha outside beta strand inside</p><p>all beta= no cross-over connections seen, us. right hand,</p><p>twisted beta sheets are more stable</p><p>some are all alpha folding, some are mixed</p>
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d. The difference between family and superfamily

family= high degree of similarity btwn primary and or tertiary structure and function

superfamilies= 2+ families with a high degree of similarity in motif and function, but less similarity of primary structure

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e. What is meant by domain

are parts that are independently stable in a protein

pep > than aa in size, can fold into 2+ domains w/ separate functions

more efficient for cat. 1 part may be for the AS while 1 is regulatory

1 subunit can regulate entire protein

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5. Define / Describe what is meant by 4°structure, the various types of 4°structure, and the roles such proteins play in a cell

multi peptides with multi subunits

us. have complex multistep functions

can do cat. of things that are different but relate to the same function

us act unit by unit

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Explain what is meant by intrinsically disordered proteins, how their properties differ from structured proteins, and some of their recognized functions

intrinsically disordered proteins lack hydrophobic cores

not all proteins are entirely defined

have an increased density of charged AA

ranked with PONDR (predictor of naturally disordered regions) score

can be scavengers = bind to ions, small molecules, reservoirs, garbage dump, insulators, inter rxn networks

p27= main cell protein kinase to inhibit cell division (would find lower [] in tumor cells)

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Explain what is meant by proteostasis including pathways that contribute to proteostasis

proteostasis= the continual maint. of proteins in a cell

synthesis, folding, native state, unfolding, refolding, denaturation

<p>proteostasis= the continual maint. of proteins in a cell</p><p>synthesis, folding, native state, unfolding, refolding, denaturation</p>
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2. Describe what occurs during denaturation of a protein and explain how heat, pH, organic solvents, and detergents result in denaturation of a protein

loss of 3D structure/ conformation decrease function in denaturing

temperature disrupts H-bonds

loss of H+ changes charge which causes denaturation

organic solvents (etOH, acetone)/detergents change hydrophobic interactions

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  1. Define renaturation

if DS bonds are broken into Cys res by urea/ mercaptoethanol they can be put in an environment that removes those toxins so the DS bonds can reform back to active/native state

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4. Describe how polypeptides / proteins are folded including hierarchical modeling

from primary structure, secondary forms next, alpha helix forms faster, beta sheets, weak interactions are the most important then ionic, finally domains are combined

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what are 2 enzymes often needed for folding

PDI (protein disulfide isomerase) needed for folding sometimes

PPI (peptidyl proyl cis-trans isomerase- converts btwn cis and trans forms of proline)

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the role of thermodynamics in protein folding

therm is represented by funnels where the bottom shows the native lowest free E state, raised areas show stability of intermediates/ possible conformations, peaks show less stable intermediates but where present show more stability

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what is the role of molecular chaperones

chap= react w/ partially or unfolded proteins to create a microenvironment for folding, also block newly formed proteins from aggregating, keeps proteins separate

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what is an HSP

HSPs (heat shock proteins) prevent proteins from aggregating under high temperature

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what do the examples of HSPs in e. coli do

in e. coli, HSP70 is open when ATP is bound and has low affinity, but closes when HSP40 binds and ATP leaves which then increases affinity to move hydrophobic regions of proteins together to prevent aggregation

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  1. Describe what a proteasome is,

large protein complexes that degrade unneeded or damaged proteins (found in most orgs)

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the basic structure of the 26s eukaryotic proteasome,

top and bottom is 19s subunit that houses the docking site where polyubiq with protein attaches to the proteosome

alpha subunits next to it are where ATPases are and need ATP to work

beta in the middle is the active site where catalysis happens

alpha and beta subunits make up the 20s core

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how it works to break down a protein (proteolysis),

(4+ ubiquine) polyubiquinated proteins move the protein to the proteosome

enter the docking site, ATP enters the ATPases at the alpha subunit, protein moves to beta subunit

ubiquitin is removed then unfolding happens

long seq of ala/ gal inhibit unfolding

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what sites are needed in the beta subunit to cleave sites on a protein

sites for threonine dependent nucleophilic attacks to break proteins in certain locations

chymotrypsin like- cleaves peptide bonds on CA side of trp, try, phe (aromatic)

trypsin like- cleaves pep bond on CA side of lys and arg (except when pro is next!)

peptidyl glutnyl- hydrolyzing like- cleaves CA bond immediately after acidic or branch chain aa

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6. Explain how a protein is targeted (or not) for degradation

Degron (amino end terminal) signals for faster or slower degradation, PEST (pro glut ser threo) signals, TF Grn4P reduces 1/2 life too

intrinsically disordered proteins don’t need a signal but Cyclin B does

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name the three enzymes and their functions in the ubiquitination process

E1= ubiquitin activating enzyme

E2= ubiquitin conjugating enzyme

E3= ubiquitin ligase

carboxyl group reacts with SH group on E1 and ATP to give off pyrophosphate

E2 transfers itself where E1 was

reacts with E3 and amino end of Lys of the target protein so that now enzymes are gone but target protein attaches (does this 4 times thru ubiquitin elongation)

ligase attaches to epsilon aa

<p>E1= ubiquitin activating enzyme</p><p>E2= ubiquitin conjugating enzyme</p><p>E3= ubiquitin ligase</p><p>carboxyl group reacts with SH group on E1 and ATP to give off pyrophosphate</p><p>E2 transfers itself where E1 was</p><p>reacts with E3 and amino end of Lys of the target protein so that now enzymes are gone but target protein attaches (does this 4 times thru ubiquitin elongation)</p><p>ligase attaches to epsilon aa</p>
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7. Describe what amyloidoses are and give specific examples that are known or suspected

E3 malfunction so can’t attach target protein to ubiq

(HPV has too much ubiq so destroys p53)

disease from improper folding/ misfolding

insoluble fibers (amyloid fibers/ plaques) increase the number of ordered structure like beta sheets so abnormally folded proteins recruit correctly folded proteins into the wrong form

type 2 diabetes can be caused by amylin when secreted by the pancreas it has a synergistic affect with insulin and forms fibers so beta cells apoptosis and insulin decreases

alzheimer’s has increased levels of beta-amyloid fibers

amyloid pre-cursor in neurons is the protein APP which which can be proteolyzed which causes prion diseases which result from an increase in beta sheets and alpha helix

parkinsons is a maybe

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Recognize and describe different methods of protein isolation/separation and characterization including: a. Salting out

1st- make crude extract (cell lysis)

2- homogenize material

3- use differential centrifugation to make subcellular fractions

4- fractionations- separate proteins in groups by density

salting out: ppt out proteins in a sol’n of (NH4)2SO4 and centrifuge to get a pellet

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separate protein from small solutes by putting them in a bag of a semi-permeable membrane that will let the small solutes diffuse out leaving the protein behind

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c. Column chromatography

shows the protein’s charge, size, and capacity to bind to other molecules

protein is in reservoir where it is pumped in a buffer to columns where higher affinity proteins stay at the top while lower affinity sub move faster and have a lower retention time

when moving it is in the mobile phase and when attached to the porus matrix it is in the stationary phase

a detector notes to a recorder and a fraction collecter collects to liquid

doing all types will increase the activity (total units of an enzyme in sol’n/amount of space, high activity= more pure)

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ion exchange column chromatography

shows differences in magnitudes of charges

keep buffer at a certain pH (can change pH to release if know pI)

allow protein to move down

beads (resin is neg) are charged and opposite charges move most slowly while same move more quickly

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size-exclusion column chrom

porus beads allow for small proteins to go through tunnels in them so they move more slowly down the column than larger beads

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affinity column chrom

ligand is attached to beads and protein is allowed to go down and speed is determined by affinity for ligand

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high performance liquid chromatography (HPLC)

uses pressure pumps to move protein down at a specific flow rate

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d. Electrophoresis

used to separate and analyze but not purify bc enzyme will no longer be in native state when done

uses charge and size, migration speed is directly proportional to strength of the net charge of molecules

polyacrimide gel electrophoresis (PAGE) is used with detergent

simple PAGE keeps it in the native state but SDS PAGE disrupts the non-cov bonds (1:1 SDS: protein molecule ration)

makes a uniform rod shape and denatures so original charge doesn’t matter

so each protein will have a similar charge:mass ratio so bigger molecules will be more negative and move faster

more purified protein will have a more defined band

can be used to make a standard curve

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e. Isoelectric focusing

separates protein by pI values. puts protein in a pH and electrical field gradient and will stop moving when reaches its pI point bc electrically neutral

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f. Two dimensional electrophoresis techniques

do isoelectric focusing and put on a strip on gel and run it on SDS PAGE thru electrophoresis to sep by pI and size each dot seen represents a protein

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2. Explain what is meant by activity and specific activity

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3. Describe how amino acid sequence/composition and structure can be determined

use purified sequence

can tag amino end using FDNB which cleaves at the amino end of Lys to breakdown larger peptides

use Cyanogen Br to cleave the C end of Met

use dift proteases to bd protein

put the sequences together

edmund degredation sequences aa are cleaved and ID’d one by one

mass spec finds a mass: charge ration for each fragment

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which amino acids do the following reagents cleave on the C terminus


submaxillary protease


S. areus

cyanogen bromide

Lys Arg



Asp Glu


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which amino acids do the following reagents cleave on the N terminus



Asp Glu

Leu + aromatics

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how to measure activity

monitor unknown rxn and compare to known rxn with a standard curve to see how active it is

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find protein []

use spec and Lowry argent for color

Coomassie blue makes it all blue dye loses protons when bound, so can make standard curve to see [ ]

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5. Solve problems utilizing the various methods


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Describe the common aspects of non-enzymatic functions of proteins particularly interactions involving  changes in conformation caused by ligand binding to a protein.

binding to a ligand us. is reversible due to conformational changes

protein AS are specific in size, charge, and shape

binding sites become more complimentary to protein after a conform change causing an induced fit so the ligand and protein bind more tightly

if there are multi sub for one protein, they will work in a regulatory process where the conformational change of the first allows for the next to work

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describe the structure of myoglobin (which is monomeric)

has 8 alpha helix subunits and one heme group

it has a heterocyclic ring derived from porphyrin with 4 pyrole groups

protein portions prevent permanent binding but when removed, binding is permanent

heme group interacts with 4 N ligands in they pyrole groups that are found on the same plane, the 5th ligand interacts with the His93 imidazole side chain which slightly displaces the Fe from its plane, the 6th ligand will bind to O2

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how does myoglobin work

when O2 binds to the 6th ligand it pulls back from the plane when not bound

Fe2+ can be oxidized to Fe3+ or metmyoglobin

metmyoglobin can no longer bind to O2

CO and H2S bind to myoglobin better than O2

its O2 sat. curve is a regular MM curve because it is monomeric and thus does not bind O2 cooperatively

is not as sensitive to changes in O2 and better for O2 storage bc of high O2 affinity

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describe the structure of hemoglobin (which is tetrameric)

subunits alpha 1 and beta 1 interact well and alpha 2 and beta 2 interact well but alpha/beta 1 and alpha/beta 2 don’t

has 2 conformations

T state (unbound) R state (bound)

T= his HC3 part is found on the outside

R= his HC3 found in the center

R has a higher affinity for O2 than T

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how does hemoglobin work

in lungs: in T state where binds to 1 O2, and conform change allows for rest of O2 to bind

enters the R state

goes to the body tissues: where it looses 1 O2 and then a conformational change allows for all others to leave

enters the T state

T state is more stable than R state where subunits slide and rotate more easily for conformational changes

its O2 sat. curve is a sigmoidal MM curve because it is tetrameric and can bind O2 cooperatively

is more sensitive to O2 changes and better for O2 transport bc of lower O2 affinity

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Explain how Kd is derived and the information that Kd provides

if Y= total number of binding sites occupied/ total binding sites aka ( [PL]/([PL] +[P]))

Ka is the association constant and Ka [L][P] can be sub for [PL]

at Y=.5 half of the binding sites are occupied and is known as 1/Ka or Kd (M) Kd= kd/ka

Y= [L]/([L] + Kd)

Kd= [P]*[L]/[PL]

therefore when [L] = Kd half of the ligand binding sites are occupied

when [L] is less than Kd, less protein is bound to ligand

lower Kd= higher affinity of ligand for protein

the more tightly a protein binds to a ligand, the lower concentration of ligand is needed for half of the binding sites to be occupied which means a lower Kd

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Predict which molecule has a higher affinity for a protein when the Kd for various ligands is known

lower Kd means higher affinity

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Recognize the structure of a heme including the different components

iron in the center w/ 4 pyrrole groups around it

Fe is planar w/ pyrrole groups when no O2 is bound and impacts the distance btwn the distal His

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Distinguish between different models of cooperativity

cooperative binding is seen when a sigmoidal curve is made and means that the complex can be more sensitive to small changes in O2

MWC says that all substrates at any given time are in the same conformation so an equal chance for ligand to bind to any (all or none)

cooperative binding in sequential method says that a conformational change in one subunit makes it more likely to be bound which then impacts the binding of the next subunit in a more sequential manner

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Describe the role BPG plays in O2 binding

hemoglobin has binding sites for CO2 and H+

CO2 needs to be converted to bicarb via carbonic anhydrase or it would bubble out this means that the pH will decrease in this process

when pH in tissues decreases, more O2 can be released so the affinity for O2 will increase in the lungs

BPG binds to the T state to stabilize it so that the affinity for O2 is lower so that at high altitudes O2 can be released (a person from higher altitudes will have more BPG)

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Identify heme (not including myosin and hemoglobin) based O2 binding protein as well as non-heme O2 binding protein, indicate where they are found, and how they are unique


Leghemoglobin= binds to O2 so that bacteria is able to do nitrogen fixation

chlorocruorin= green in annelids


found only in inverts

hemerythrin= 2 Fe and intracellular protein

hemocyanin= blue extracellular O2 transporter in mollusks and arthropods that binds to copper

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