Test Three final review

involved in denitirification and the urea process

break the S-S bond; run through cesium chloride; then centrifuge and separate products--> assay

• before: only one peak
• after assay: breakdown-- 2 peaks= r2, c3

T state: it is compact; the two lobes are bound by a hinge and they are held by ionic bonds between the amino acids; no space in the middle; side chains are too far apart

R state: side chains are farther apart; two lobes close and the substrate fits in, allowing active site to be active; the lobes are held within the intramolecular bonds; pull apart and rotate

produces cAMP

four bind to the regulatory sites

thrombin formation from prothrombin, which activates fibrinogen into fibrin, which forms a soft clot by cross-linking of lysine and glutamine by transglutaminase

• responsible for cutting bonds int he alpha helical rods of fibrin
• contains two kringle domains, a serine protease domain, and a fibrin binding domain

this is the final step of the cascade

cleavage of four glycine arginine bonds in the central region is going to release the A and B fibrinopeptides. A fibrinogen without these is a fibrin monomer. 

The fibrin monomer is now capable of polymerizing into fibrin. The fibrin monomers come together to form fibrin. The homologous B and gamma chains have globular domains and holes at the ends that interact with peptides. A knobs fit into gamma holes to form protofibrils, which can be extended by beta subunits associating with other beta subunits. The newly formed soft clot is stabilized by formation of amide bonds between the side chains of lysine and glutamine

still capable of dividing and proliferating

signals production of transcription factors, which eactivate genes for proliferation and activate all muscle specific proteins; key role in regulating muscle differentiation

six polypeptide chains

the elongated chains form alpha helical coiled coil and do not have proline nor do they have kinks. There's a repeat of seven amino acids: ABCDEFG; and And D are hydrophobic, BCFG are charged.

A and D always end up on the same side, allowing them to hide out int he helix. The charged ones lie on the utside.

reinforces and gives strength during conformational changes

uses it to polymerize

directional with plus and minus end; in sarcomere, it is unidirectional 

myosin is bipolar

polar

region of the myosin which contains the S1 and S2 regions

reorientation of the lever arm

little movement in the Ploop translates into slightly larger movement as switch I and II adhere tightly around the gamma phosphoryl group. This is going to cause conformation change in relay helix and thus movement of the lever arm

t has the TnC, TnI, and TnT regions

TnT is a tropomyosin-binding subunit which regulates the interaction of troponin complex with thin filaments

TnI inhibits ATP-ase activity of acto-myosin; interacts with tropomyosin; conformational change leads to movement of tropomyosin away from the binding site that myosin can now bind to

TnC is a Ca2+-binding subunit, playing the main role in Ca2+ dependent regulation of muscle contraction

gives structure to cell with no cell wall

railway for communicatin system/ cell unit

made of keratin; comes together in multisubunit helices like collagen

microtubule organizing center; binding point for first subunit. Individual subunits polymerize outward.

bundle of microtubule fibers and other associated fibers that is continuous with teh membrane; euk flagella is anchored by it

connects parts of microtubules to each other in the axoneme

the ATPase located all up and down the flagellum

gets ATP in active site

reaches out to next MT

grabs it

hdrolyzes ATP

conformational change--> power stroke

has affinity for MT; affinity changes whether ATP or ADP is in active site

P loop, switch I and II, relay helix attached to neck linker

Chemorepellnt binds to receptor on membrane, triggering a kinase adn overphosphorylation, which causes continuous tumbling.

with a conformer, your body will introduce more unsaturated fatty acids

to develop a permeability scale; if you carry a charge, you don't get through with ease

Hydrophobic molecules have an easier time

a transmembrane protien

it is lodged in the membrane/ detects damage to the membrane 

• 2 step reaction: cyclooxidase and peroxidase
• 1) converts fatty acids and all and converts it to hydrophilic molecule that signals pain and swelling associated with damage

GPI anchored proteins? 

addition of hydrophobic groups to associate the protien to the member (like prenyl groups to help anchor)

It increases the period of time recovering

due to Na+-K+ concentrations

• inside: high K concentration
• outside: high Na concentration

Na and K flow through the channel and depolarize the membrane to the point where there is no charge difference.

you need to isolate via affinity chromatography; contains snake venom that binds to the receptors and inhibits its funciton

pentamer of four different subunits; 2 alpha, one beta, one gamma, and one sigma

side chains associated with the alpha helix extend through the channel and block

You go into the cell that has acetylcholine receptors and use a glass pipette to grab the piece fo membrane with receptors. 

Another way is going into the cell and poking a hole

an electrode is stuck inside nad outside the pipette. A voltage is applied and the current is mesured. Depending on resistance, the current will change. 

Result: when channels close, the current needs to pass through the membrane. High resistance. 

When the channels open, there is lower resistance and it goes in easiy

Suction leads to a gigaseal forming-->

1) suction: whole cell mode: everything flows out; we have to supply NT outside of pipette

2) excised-patch mode: inside out--we're removing other part; clog up the tip of the pipette with top or bottom view; apply NT inside pipette

affinity chromatography with tetrodotoxin, which binds th Na channels to prevent function

new set of charges as S4 rotates up out of the membrane

there are positively charged side chains ner the constriction site to prevent movement through

concentration gradient: allows diffusion across membranes

membrane potential: charged disparity--> requires energy input to create charged disparity

at the core of the protein is an aspartic acid residue that gets phosphorylated

protein bacteria use to get lactose in cell

move lactose against gradient/ requires energy; proton gradient that exists across abcterial cell membrane