Term
|
Definition
*AA seq of polpeptide chain
*help understand 2, 3, 4
*form all other seq
*20^n possible residues, only some chains exist b/c some do something, others don't
*most shared of these are protein domains |
|
|
Term
|
Definition
*combo of AA
*can have A + B chain |
|
|
Term
|
Definition
*in nucleotide seq= change in primary structure
*leads to new AA seq, new 1 struct
*change 1 letter changes struct + func
*EX: DCN (norm), CSCD (mut); - impact |
|
|
Term
|
Definition
*mutation causes unorganized collagen arragnement
*light cannot ass through to retina
*broken areas cause light to bounce back
**knockout 1 nuc = change in 1, 3 struct |
|
|
Term
|
Definition
| *many look closely resembled b/c essential for life and highly conserved (seq, struct) |
|
|
Term
|
Definition
| *random mutations that do not affect function |
|
|
Term
|
Definition
*strut of AA cannot be changed
*homologous prot that are essential to func, conserved
*cannot change b/c important across all species (#1s) |
|
|
Term
| Conservatively substituted |
|
Definition
*residue that could be replaced and still serve original AA role
*another residue can accommodate
*can be changed only if it does not change overall struct
*any nonpolar R group can work and might not affect it
* few changes (2,3,4) |
|
|
Term
|
Definition
*any AA replacement allowed
*subject to neutral shift where placement of AA dos nothing
*can change, just a placeholder |
|
|
Term
|
Definition
*depict history of AA seq
*less diff = more closely related
*bottom tree = sm diff, top= lots |
|
|
Term
|
Definition
*40-200 AA residues (1000-1400 fam)
*40% AA identity indicates identical func
*func could be sim even with diff seq
*in struct terms, struct is defined by domain |
|
|
Term
|
Definition
*homologous protein w/ same func in diff species
*ID as the same and have sim func |
|
|
Term
|
Definition
*genetic recomb event that leads to a 2nd copy of that gene, a duplicate, in the genome
*2 of the same, something mutates causes protein to be sim but diff func
*leads to paralogous gene |
|
|
Term
|
Definition
*gene evolve independently after a gene duplication event
*one gene gains new func |
|
|
Term
|
Definition
*the rate at which mutations get accepted into a protein (varies)
HISTONES |
|
|
Term
|
Definition
*usually cell-cell interactions, lots of change
*change rapidly because mutate a lot
*as new roles needed, these take charge
*many domains (multidomain protein) = many roles |
|
|
Term
|
Definition
*local, spatial arrangement of polypeptide backbone atoms w/o regard for side chains
*3D for of local segments of protein
*backbones of AA (everything but R group)
*how to get 3D struct from 1, work on backbone
*rigid, planar, peptide bond w/ backbone
*trans favored (C-N, 1.33; C-N, 1.46; 1st has more E)
*pro favors cis, so has some 2*
*seq of residues w/ repeating ψ,φ value
*favorable H-bond and ψ,φ
*a-helix, B sheet, B bends, loops |
|
|
Term
|
Definition
* most conserved b/c essential for life (help org DNA/ binding; same across all org)
*shows that genes have a stable role |
|
|
Term
|
Definition
*proteins can have combos of domains
*allows to mix & match to get a good protein |
|
|
Term
|
Definition
*the 3D form of an entire polypeptide, including side chains
*interactions between R groups
*helices w/ R groups outward cause react and form another structure
*folding of 2* elements that combine to form motifs and domains |
|
|
Term
|
Definition
*the spatial arrangement of a protein and its subunits
*put proteins into lrg protein
*spatial arrangement of polypeptide subunits
*EX: 4 separate units of hemoglobin assembled into a oligomeric protein |
|
|
Term
|
Definition
*cause by series of double bonds
*have rotational groups |
|
|
Term
|
Definition
*sterically constrained (certain angle combos cause collisions)
PHI (φ)
*torsion angle around the Cα-N bond
PSI (ψ)
*torsion angle around the Cα-C bond |
|
|
Term
|
Definition
*tells optimal angles for ψ,φ
*angles common and repeated make them possible
*can't exist when molecules bump
*every AA has ψ,φ, but when you get to space where both exist -> 2 struct |
|
|
Term
| Reading the Ramachandran Diagram |
|
Definition
BLUE
*easily allowed bond angle combos
*ee B-sheets, collagen triple helix, a-helices
*most common
GREEN
*more crowded, outer limit bond angle combos
GRAY (EVERYTHING ELSE)
*least allowable/ unallowed angle combos
EX:
Glycine- symmetric, take many angles b/c simple
Proline- only in specific ψ,φ angles
*all help define shape to find regular 2 struct |
|
|
Term
|
Definition
*right handed coil (3.6 residues/turn)
*pitch: 5.4 A, 12 resides = 18A
*back bone Hbonds: C=O (nth residue) points along axis toward the peptide N-H group(n+4)
*avoid steric hinderance with side chains out and down |
|
|
Term
|
Definition
| how much distance rises per turn |
|
|
Term
|
Definition
*use H-bond of backbone between neighboring polypeptide chains
*pleating caused by orientation of backbone (side chains extend to opp sides sheet)
*2-22 strands sheets = 15 AA residues e
*angles allow Hbond to cross chains in polypeptide
ANTIPARALLEL
*stronger bond b/c lined up
*AA N-C going opposite
*need to 1st reach B bend that reorients the seq
*need to first reach loop
PARALLEL
*AA N-C goes same direction
*less stable b/c distortion of H bond |
|
|
Term
| Bovine Carboxypeptidase A |
|
Definition
*both parallel + anti
* R hand twist b/c L-AA chirality
*topology complex |
|
|
Term
|
Definition
*depends on morphology
GLOBULAR
*H2O soluble
*compact, highly folded struct
*majority of proteins
*several types of regular 2 struct (denatured, native)
FIBROUS
*stiff, elongated confirmation
*forms fibers (keratin, collagen) |
|
|
Term
|
Definition
*durable, unreactive
*a keratin: mammals, B keratin: birds
*a keratin looks like a-helix but not (shorter pitch, 3.5, because coiled coil)
*abcdef tetrads = ad nonpolar residues(4*)
*rich in Cys residues
*disulfide links- tell hard/soft (curly lots) |
|
|
Term
|
Definition
DIMER
2 keratins (1 ind)
PROFILAMENT
2 columns of dimers (2 columns of multiple ind, 1 tube)
PROTOFIBRIL
2 columns of protofilaments (2 tubes that form 1 medium tube, 4x)
MICROFIBRIL
4 columns of protofibrils (4 medium tubes together = 1 big tube) |
|
|
Term
|
Definition
*most abundant vertebrae protein
*strong, insoluble stress bearing fibers (conective Tiss)
* 1 molecule = 3 polypep chains (helix)
*28 collagens b/c combos og genes working @ 1 time e, prod a subunit
*3000 A long, 14 A wide
*1/3 Gly, 15-30% Pro/ hydroxy(Pro/Lys)
*repeating AA (Gly- Pro(X)-Hyp/Hyl (Y)
*L handed polypetide(3 residues.turn) b/c Pro prevent a helix (lack backbone N-h for Hbonds) -> R hand triple helix
TYPE 1
2 a1(l) + 1 a2 (l)
*coded by COL1A1, COL1A2 |
|
|
Term
|
Definition
*requires propyl hydroxylase and ascorbic acid (VC)
*mod proline cause scurvy |
|
|
Term
|
Definition
*every 3rd residue of e chain asses center of trple helix
*only Gly fits -> peptide groups orient so N-H (Gly) can H bond w/ carbonyl (Pro)
*rigid struct = tensile strength (gives strength, struct; turn one way get tight, vice versa)
*older collagen = cross linked (not Cys based) -> allows 4 side from Lys + His to covalent bond
*w/ R hand helix, R groups point in |
|
|
Term
|
Definition
DENATURED
fully unfolded protein
NATIVE
*folded
*nonrepetitive struct no less ordered than helices/ B sheets
*more irregular, difficult to describe |
|
|
Term
|
Definition
DISTORT REG CONFIRMATION
*variatins in AA seq
*overall struct
*extar residue (B buldge)
*Pro- kink in a helix, B sheet
*sev AA resid w/ lrg side destabilize ahelix
PRESENCE OF SOME RESIDUES= NONRANDOM
*@ end of helices form caps (Asp/Glut) stabilize/assist Hbond |
|
|
Term
|
Definition
*side chains in globular are distributed by polarity
NONPOLAR
interior of prot bc trying to escape water
CHARGED POLAR
protein surface in contact w/ aqueous
UNCHARGED POLAR
either (inside: H bond w/ others_ |
|
|
Term
|
Definition
nonpolar on inside
HEME: prosthetic group |
|
|
Term
|
Definition
* AKA super secondary structure
*few 2* structures together
*BaB, B haripin, aa
*need several to produce domain
* create struct w/ diff shapes & gaps (molecule flow in)
*STRUCT CONSEVED MORE THAN SEQ
**recognizeable subcomponent of the fold |
|
|
Term
|
Definition
*glob clusters give proteins bi- mitobular look
*40-200AA
*usually has layers of 2* & own func
*area where 2* forms super 2*, and super 2* come together and form spot
GAPDH
has diff domains 1) binds NAD 2) binds glycealdehyde-3-phosphate
*act of folding = 3* |
|
|
Term
|
Definition
*sheets make spot for DNA to interact
*used for trasncription
*motif allows to fold in 3* |
|
|
Term
|
Definition
*DNA clamp
*processivity factor for DNA polymerase in euk cells
*essential for replication |
|
|
Term
|
Definition
*form stable folding patterns
*tolerate AA delete, subs, insert
*support essential biological func
*compact and self folding component of protein that represents a discrete structural / functional unit |
|
|
Term
|
Definition
*used differently in contexts
*reproducible and recognizable 3D arrangement |
|
|
Term
| Benefits of Quaternary struct (multisubunit prot) |
|
Definition
*defects can be reapired by replacement
*site of mnufacturing diff from site of assembly
*utilized diff
*subunit assembly/interchanging basis of regulation (come together have job) |
|
|
Term
|
Definition
SUBUNITS ASSOCIATE NONCOVALNTLY
*oligo, protomers
*contact regions between subunits resembel interior of sing subunit (close pack nonpolar chains, Hbond back +side, interchain diS)
SUBUNITS SYMMETRICALLY ARRANGED
*e protomer occupies a geometrically equivalent (have pattern/shape) |
|
|
Term
|
Definition
OLIGO
proteins w/ more than 1 subint
PROTOMERS
identical subunits in a protein
(EX: Hb dimer of aB proto) |
|
|
Term
|
Definition
GREATER SIDE CHAIN HP
more likely to occupy protein center
LESSER SIDE CHAIN HP
*less likly to occupy protein center
*transmembrane along line
PLOT: hydrophob- top, phillic- bottom |
|
|
Term
|
Definition
1)Hydrophobic affect
2)Site Directed mutagenesis
3)Electrostatic interactions
4)Disulfide bonds
5)Metal ions |
|
|
Term
| STABILITY: The Hydrophobic effect |
|
Definition
*greatest influence (determinant of native struct)
*nonpolar min contact w/ H2O + inc entropy
*major determinant of native
*nonp side in allows cages frooomed around hydrophobic
*allowing to fold/ more exchanges protein = dec entropy
*hydropathy |
|
|
Term
| STABILITY: Site Directed Mutagenesis |
|
Definition
1)HYDROPHOBICITY OF SUBSTITUTED RESIDUE
*if change to phillic, change structure greatly
*mutation affects phobicity
2)SUBSTITUTED RESIDUES STERIC COMPATIBILITY
*b/c R group bigger, makes hard to fold
3)VOL OF SIDE CHAIN
*if too wide, occupy wrong space |
|
|
Term
| STABILITY: Electrostatic Interactions |
|
Definition
VANDER WALLS
*If you disrupt Vanderwalls, protein unfolding and molecules moving further away
* once denatured, Hbond lost and forming w/ H2O, easily manipulated spread apart so can't interact anymore
*minor contrib b/c bond w/ water: sm diff in free E, e. Hbond provides stabilizing E, 3* structure selects for stable
SALT BRIDGE ION PAIR
*minor contributor |
|
|
Term
| STABILITY: Disulfide Bonds |
|
Definition
*cross-link extracellular proteins
*lock in folding pattern, extracellular b/c low pH
*can lead to same folding conformation |
|
|
Term
|
Definition
STABILIZE SM DOMAINS
*attracts charged side groups to center to put into R
*provide favorable shape and give function (domain)
*EX: Sinc Fingers- involved in DNA binding, cause protein to maintain fold |
|
|
Term
|
Definition
*caused by low conormational stabilities
*adding high E, High S
*more S because occurrences w/ H2O
HEATING
*affects conformation, entire polypeptide unfolds/melts
pH
*alter ionization states of AA residue side chains, changing chrge distrib + Hbond
DETERGENTS
*associate w/ nonpolar residues, interfering w/ hydrophobic interactions needed for native struct
CHAOTROPIC AGENTS
*ions or small organic molecules that inc solubility of nonpolar substances in water
*inc chaos/disorder/entropy
*EX: Guanidinium ion + urea look alike and have good denaturing capabilities |
|
|
Term
| Anfinsen Model of Denaturation/ Renaturation |
|
Definition
1) Native : add urea + mercaptoethanol (cleave DiS)
2)Denatured:
a.remove both, folds w/ O2 (native, active)
b.remove MCE, partial unfolded (allows Dis reform)
3)
b.PARTIAL UNFOLD: enzymatically inactive, DiS bonds at random (scrambled)
4)
SCRAMBLED: adding MCE no O2 catalyzes and allow DiS to form (goes to Native a.)
**In order to recover, need to watch MCE, can't do MCE 1st b/c form and lock DiS in wrong place |
|
|
Term
|
Definition
| *constantly moving/ shifting in place |
|
|
Term
|
Definition
*on own, can't tell struct; when bound you can
**EX: CREB |
|
|
Term
| Folding Pathway: One-Way process |
|
Definition
*as folding occurs, conformational stability increases
1)Goes from 1* to local segments of 2*
2)Hydrophobic collapse (phobic interact draw protein close together) -> molten globule
3)b/c collapse, 2* struct stabilizes to 3*
4) FORMS SUBDOMAIN (REGIONS OF DOMAIN)
5)Complex rearrangements could still have H2O regions so need to expel
6)assembly of multidomain/subunit (could go to 4*) |
|
|
Term
Energy-Entropy Diagram:
Protein Folding Funnel |
|
Definition
*high E, S -> low E, S (native
*^S < 0 but ^H losing E (<0)
*^ H is so - that ^G<0 (spont)
DOWN DIAGONAL: renature (release E into surrounding, E leave system)
UP DIAGONAL: denature (gain E in syst/ providing E to break bonds)
DIPS: struct stabilize momentarily; interaction occurring testing if able to break bonds) |
|
|
Term
|
Definition
*bind and shuttle proteins around
*prevent it from being active in wrong location |
|
|
Term
| Protein Structure impact on func |
|
Definition
ALLOWS TO REVERSIBLY REACT W/ MOLECULES
-specific interactions- protein discriminates molecules
SEPARATE BINDING SITE FOR LIGANDS
*extra complementary w/ coupling to a conformational change (induced fit)
PROTEINS FLEXIBLE
*whatever happens is essential for protein
*subtle, dramatic changes in conformation
*Multisubunit proteins, one conformational change cause another-> changes in whole unit
EX: Mb, Hb |
|
|
Term
|
Definition
*molecule that binds to a protein
*usually fits right into portien shape
*has opposite charge to attract or will hace phillic/phobic character
*some sites that don't fit are not effctive |
|
|
Term
|
Definition
*where ligand binds
*complementary to ligand in shape, size, charge, phillic/phobic character |
|
|
Term
| Rate of gas exchange affectors |
|
Definition
1)THE AREA AVAILABLE FOR DIFFUSION
*SA
2)THE DISTANCE OVER WHICH DIFFUSION OCCURS
*how thick is diffusion area
3)THE [] GRADIENT ACROSS GAS EXCHANGE SURF
*greatest -> least
4)THE SPEED AT WHICH MOLECULES DIFFUSE THROUGH THE MEMBRANE |
|
|
Term
|
Definition
1) Lrg SA:V
2) Thin
*circulation helps thicker (>1mm)
3) Mechanisms for maintaining steep [] gradients across themselves
4)Permeable to gases
*single celled org |
|
|
Term
|
Definition
*1 protein subunit struct
*8 a-helices
*globular
*heme group w/ 6 ligands
*facilitates O2 diffusion in musc
*holds O2 so cell can pull more from cytoplasm = more diffusion + Oxy |
|
|
Term
|
Definition
*makes blood red
*extra molecule, w/ Fe, exists to help protein
*has high affinity to bind O2 but also CO, NO, H2S (toxic)
IN Mb
*wedged in hydrophobic pocket between E and F helices bound to Fe |
|
|
Term
|
Definition
*causes heme heterocyclic ring system
*4 modified pyrrole (combo of 5rings w/ C=N) subunits
*interconnected at a-C by methene bridges (N bond w/ Fe) |
|
|
Term
|
Definition
1) Pyrrole A
2) Pyrrole B
3) Pyrrole C
4) Pyrrole D
5) His F8
*8 AA in F helix
6) Fe(II):O2
*His E7 Hbonds to O2
*O2 important b/c side group can easily change charges (Val +Phe give barrier so O2 can flow in + prevent going elsewhere)
*allows O2 to bond irreversibly (allows musc to take in more O2 as needed)
*O2 alters electronic state (discolored meat b/c irreversible bond form) |
|
|
Term
|
Definition
1) O2 diffuses from capillaries to tissues
2) Low solubility in aq soln
3) Mb stores O2 on Fe (II) of heme
4) Less O2 in aq soln so diffusion from high [O2] -> low [O2] w/ more O2 stored in Mb |
|
|
Term
|
Definition
*[Mb] aquatic > [Mb] terrestrial
*b/c greater demand for O2 storage
*Endurance caused by 1) inc #s Mb 2) net charge (+) cause Mb repulse + spread out |
|
|
Term
|
Definition
|
|
Term
|
Definition
*W/o it, Fe(II) irreversibly bind w/ O2
*Mb protein prevents oxidation and allows to bind reversibly |
|
|
Term
|
Definition
*4 heme groups like Mb (3* struct) together
*dimer of aB protomers x 2 = tetramer
*highly symmetrical
*O2 binding alters structure of entire hemoglobin
*His E8 of Fe, His E7 on O2 |
|
|
Term
| Hemoglobin Conformational States |
|
Definition
DEOXYHEMOGLOBIN
*release more O2 (heme low affinity bind O2)
*when O2 bonds causes changes
*allow molecule to know to get rid of everything
*T State (tight)
OXYHEMOGLOBIN
*bind more O2 (high affinity)
*R state (relaxed) |
|
|
Term
|
Definition
*the binding of a ligand to one site affects (inc affinity) the binding of additional ligands to other sites
*the fourth bonds w/ 100 fold greater
*info about binding being gathered by entire structure |
|
|
Term
|
Definition
*T: pulling "down," drawing F Helix closer to Heme + His F8
*R: O2 bound, relaxes and pulls away
*Fe moves + His moves w/ it and pulls on whole helix |
|
|
Term
|
Definition
*T: Asp - Thr (C6)
*R: Asp - Thr (C3)
*shows changes in 3* struct b/c 2 different subunits
*puts a,B in good places
*ion pairs only provide temporary stability |
|
|
Term
|
Definition
| *subunits are tightly coupled so that 3* structure changes cannot occur w/o 4* occurring in entire tetrameric protein |
|
|
Term
|
Definition
1) the decrease in O2 binding affinity of Hb in response to a decrease in pH
2)CO2 combines w/ N terminal amino groups of blood proteins to form carbamates |
|
|
Term
|
Definition
| *accelerates a rxn in erythrocytes by converting CO2 -> HCO3- + H+ |
|
|
Term
|
Definition
*has cells w/ organizational anatomy
*contracts individual cells to contract whole muscle |
|
|
Term
|
Definition
I BAND:
*thin filaments, isotropic (same)
*all attached to Z
*slides over thick to create diff band patterns
A BAND:
*thick filaments, Myosin, anisotropic (diff color)
*all attached to M
H ZONE:
*mid of I, huller -> brighter
Z DISK:
M DISK:
*when contract, between M+Z shrink (close together)
SARCOMERE: distance from I -> I |
|
|
Term
|
Definition
*component of thick filaments
*M disc w/ globular heads at N-term
*2 heavy 220-kD chains,
*2 pairs light chains EssentialLC, RegulatoryLC (Bind near actin)
*R hand helices w/ left hand coil (left hand coiled coil)
*heads (ATPase) form cross bridges to thin
N TERM (head/ATPase)
in between myo and actin
C TERM (a-helical tail) |
|
|
Term
|
Definition
| *on myosin head, turn ATP-> ADP |
|
|
Term
|
Definition
*component of thin filament
*most abundant cytosolic protein in euks
G-Actin
*globular, exists by itself
F Actin
*fibrous, together
*polymerization causes double stranded helix in which each subunit contacts 4 others
*forms fiber and has bind sites for Ca, Mg, ATP (not req)
*same orientation (+, - end important for treadmilling) |
|
|
Term
|
Definition
*areas myosin head binds
*e monomeric unit can bind a single myosin head
*interaction w/ actin and myosin requires level of regulation |
|
|
Term
|
Definition
*complex regulates musc contract by controlling access of myo heads on actin bind sites
TROPOMYOSIN
*wrap around actin
*give access to bind sites/ hide when not binding
*homodimer, 2 a-helix (parallel coiled coil)
*able to contact 7 consecutive actin subunits b/c form cables in grooves of F actin
TROPONIN
*alternate w/ and covers entire thin filament
*binds Ca and causes shift
*3 subunits: TnC, TnI, TnT |
|
|
Term
|
Definition
TnC
a Ca2+ binding protein
TnI
binds to actin
TnT
elongated molecule, binds to tropomyosin at its head- tail junc |
|
|
Term
|
Definition
1) when musc needs to move, nerve impulse cause Ca2+ release from Sarc (inc [Ca] in)
2)Causes troponin-tropomyosin complex to expose actins myosin head bind sites (M + Z close)
3)Dec [Ca] in b/c pumped back into Sarc by ATP requiring pumps
4) Causes troponin-tropomyosin coplex to block actin bind site (relax) |
|
|
Term
|
Definition
*holds myo and actin but doesnt play role in sliding filament model
*lrgst protein, tethers everything together |
|
|
Term
|
Definition
*cells can use actin by itself
*allows cell to crawl towards antigen (macrophage)
*microfilament treadmilling |
|
|
Term
|
Definition
1) usually + end receiving G-actin, - droppin off F- actin
2) adding to front and taking off back
3)allows movement in cell in certain direction |
|
|
Term
|
Definition
|
|
Term
|
Definition
PREP/INVEST: 2 ATP / 1 gluc (spent)
PAY/RECOVER: 4 ATP / 1 gluc (gen by subs-levelP)
NET: 2 ATP / 1 gluc |
|
|
Term
|
Definition
2 NAD+ reduce to 2 NADH / 1 gluc
AEROBIC: red coenz transrt e- to e- transprt to synth more ATP and get NAD+
ANAEROBIC: NADH needs to be reoxid by other means (homolactic) to regen NAD+ |
|
|
Term
|
Definition
*2 pyruvate molecule prod
AEROBIC: pruvate -> CO2 in CAC + ATP
ANEROBIC: metabolized to regen NAD+ |
|
|
Term
|
Definition
*Payoff phase
*2 phosphorylate C3 units transformed into pyruvates
*4 ATP prod |
|
|
Term
|
Definition
*pyruvate can go 3 ways
1) CO2 + H2O
-w/ NAD -> NADH
2)Lactate
-w/ NADH -> NAD
- homolactate ferm
3)Ethanol
-w/ NADH -> NAD
- alc ferm (not in human) |
|
|
Term
|
Definition
*pyruvate + NADH -> L-lactate + NAD
- lactate dehydrogenase oxidizes A->B
*during vigooruos activity (high ATP, low [O2]) =anaerobic glyc, not ox phosp (rapidly synth ATP)
*freely reversible ([] readily equil) |
|
|
Term
| Efficiency of Homolactic Ferm |
|
Definition
*sm of all rxn used to gen ATP
*majority gen as heat (body T) |
|
|
Term
|
Definition
TYPE 1
*mostly red (lots Mb, rich in Fe)
*musc contract sllow, steady
*maintain ATP from ox phop |
|
|
Term
|
Definition
TYPE 2
*dec Mb b/c less ox phosp, more ATP (glycol)
*mostly white
*musc w/ quick, short bursts
*devoid of mitchon |
|
|
Term
|
Definition
DUCK
*hearty flyers = slow twitch
CHICKEN
*not fliers
*rich in fast twitch |
|
|
Term
|
Definition
*yeast cells in anaerobic cond NAD regen when convert pyruvate -> Co2 + ethanol
*inc alchool content w/ sugars |
|
|
Term
|
Definition
*regulation @ huge dropoffs
*flux control for glycolysis = PFK (hexokinase b/c gluc6 eaiy bypasssed) |
|
|
Term
|
Definition
STATES:
1)T STATE
*not willing to go through glycol
*less act, dec affinity for F6P
2) R
*F6P (substrate) preferably binds
BINDING SITES
1) Substrate site
*bonds ATP equally well for e conform
2) inhibitor site
*binds ATP almost exclusivel to T
*push phosp to T = dec affinity
ALLLOSTERIC
INHIBITOR = ATP
ACTIVATOR = ADP, AMP, Fruct(2,6)biphosp |
|
|
Term
|
Definition
1) ATP acts as allosteric inhibitor of PFK by bind to T state (shifts T <- R)
*too much binds @s diff site -> confo change
2) PFK affinity for F6P dec |
|
|
Term
|
Definition
1) need more ATP
* bind at same allosteric site |
|
|
