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Uleinatructo Janus Fou Muorescently Degeu smnplc _ lideand tells >ou that protcin ~interest Ouorescesgrcen. When rou are attempting visualize Ihe protcins marked...

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Uleinatructo Janus Fou Muorescently Degeu smnplc _ lideand tells >ou that protcin ~interest Ouorescesgrcen. When rou are attempting visualize Ihe protcins marked by the grecn Hluorescence under the microscope; wlat cu light should you use illuminuethc sample?Ufeem' ; 1` ~' '| {44' 174(IRc TIMe?nr Tur A4 immunoglohulin heing Tranecrihed and there MUAIM (at rlruin substitutiun serine for isoleucine tnable rrgion of the Fah domain whut Would TuL predict is # possible cousequc

uleinatructo Janus Fou Muorescently Degeu smnplc _ lideand tells >ou that protcin ~interest Ouorescesgrcen. When rou are attempting visualize Ihe protcins marked by the grecn Hluorescence under the microscope; wlat cu light should you use illuminuethc sample? Ufeem ' ; 1 ` ~' '| {44' 174( IRc TIMe? nr Tur A4 immunoglohulin heing Tranecrihed and there MUAIM (at rlruin substitutiun serine for isoleucine tnable rrgion of the Fah domain whut Would TuL predict is # possible cousequcnce W Gnx protcin product? Jeactun The immunoglobin might not bind complement The Immunoglobulin might nOt €ystallize properly Fc Funchun €)The immunoglobulin might not bind correct e antigen There would be no change because seine and isoleucinz have similar characterislics_ Tete HOL enough informalion prediet change_ Which pair "minO aclds coult bt eunncO structurelfolding interactions much; ifatall? protein without chunging the overall ~aspurtic tenht TTrumnt DBc _ bettuming * plutumnic_jil mlethionine Cstcine HHuLG #enrtatne armathe Nline & leucine Which amino acid residue typically found structures? ~Histidine Tyrosine 1-Proline Phenylalanine Gilyceraldehyd: bends and unstructured regiuns sccontur Assumc thatyou are set of five polypeptides; each of which consists of single = amino acid Aglyeine; lysine; aspartie acid, cysteine, and alanine:) In which order would you see them sont during isoelectric focusing (theoretically): (Arranged by pH on the left side to high pH on the right side) Glycine; Lysine, Aspartic acid, Cysteine. and Alanine. Lysine. Glycine. Cysteine. Alanine, and Aspartie acid Aspartic acid, Glycine. Cysleine; Alanine. and Lysine Aspartic Acid, Cysteine, Glyeine, Alanine and Lysine Aspartic Acid, Alanine, Glycine, Cysteine and Lysine



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The nuclear pore complex (NPC) creates a barrier to the free exchange of molecules between the nucleus and cytosol, but in a way that remains mysterious. In yeast, for example, the central pore of the NPC has a diameter of 35 $\mathrm{nm}$ and is $30 \mathrm{nm}$ long, which is somewhat smaller than its vertebrate counterpart. Even so, it is large enough to accommodate virtually all components of the cytosol. Yet the pore allows passive diffusion of molecules only up to about 40 kd; entry of anything larger requires help from a nuclear import receptor. Selective permeability is controlled by protein components of the NPC that have unstructured, polar tails extending into the central pore. These tails are characterized by periodic repeats of the hydrophobic amino acids phenylalanine (F) and glycine (G). At high enough concentration $(\sim 50 \mathrm{mM})$, the FG-repeat domains of these proteins can form a gel, with a meshwork of interactions between the hydrophobic $\mathrm{FG}$ repeats (Figure $\mathrm{Q} 12-2 \mathrm{A}$ ). These gels allow passive diffusion of small molecules, but they prevent entry of larger proteins such as the fluorescent protein mCherry fused to maltose binding protein (MBP) (Figure Q12-2B). (The fusion to MBP makes mCherry too large to enter the nucleus by passive diffusion.) However, if the nuclear import receptor, importin, is fused to a similar protein, MBP-GFP, the importin-MBP-GFP fusion readily enters the gel (Figure $\mathrm{Q} 12-2 \mathrm{B}$ ). A. $\quad$ FG-repeats only form gels in vitro at relatively high concentration $(50 \mathrm{mM}) .$ Is this concentration reasonable for FG repeats in the NPC core? In yeast, there are about 5000 FG-repeats in each NPC. Given the dimensions of the yeast nuclear pore $(35 \mathrm{nm} \text { diameter and } 30 \mathrm{nm} \text { length })$ calculate the concentration of FG-repeats in the cylindrical volume of the pore. Is this concentration comparable to the one used in vitro? B. A second question is whether the diffusion of importin-MBP-GFP through the FG-repeat gel is fast enough to account for the efficient flow of materials between the nucleus and cytosol. From experiments of the type shown in Figure $\mathrm{Q} 12-2 \mathrm{B}$, the diffusion coefficient $(D)$ of importin-MBP-GFP through the FG-repeat gel was determined to be about $0.1 \mu \mathrm{m}^{2} / \mathrm{s}$. The equation for diffusion is $t=x^{2} / 2 D,$ where $t$ is time and $x$ is distance. Calculate the time it would take importin-MBP-GFP to diffuse through a yeast nuclear pore $(30 \mathrm{nm})$ if the pore consisted of a gel of FG-repeats. Does this time seem fast enough for the needs of a eukaryotic cell?

Complete it had the license off peptide yielded. Equip Melo quantities off Loosen or Norton Personal, Elhanan Pro Lean and Valley. This indicates that the different types of feminizing that the present in the Web died if the number, um so again a number of feminized it is known we can estimate the molecular weight off the peptide. Hence it is estimated Tau Bay 1200. Katie started on treating the peptide with car poxy pep 50 days. It failed to get hydrolyzed, which indicates that the car box three 50 days There's no action on this peptide car. Boxy pep. Today's high July says the car boxes terminology Step days as it has no action on the peptide. It is indicated that there are no free car boxy terminal. And for this peptide okay, Next is treating the peptide with FTN Be Regent, which is followed by a complete Heidel, isis and chromatography. It yielded free immuno assists and derivative off F N f D N b. From this structure, it is evident that the F. D. N V derivative has or nothing, and it it indicates that the end terminal ends has or anything their lives analyzes it is clear that the peptide and dominant ends is Earn Ethan and the sit down and and it's not free. Next, Uh, the DI and Tri baptized that are obtained by the partial hydro leases gives us a hint that the baptizes reputation off, you know, is it. Earlier, it was clear that this reputations are and equal molar quantities from the above step there is from the it is clear that the interminable Emine ISAT IHS or nothing on. If we observed to die peptide or anything, view, you can say that or anything is followed by loosen from the dye peptide flu. Be edgy. It is clear that Lucille is followed by finite element phe pro di that died indicated finance on an espresso, followed by the problem that dry peptide pH a pr ove l gives the information that probably is followed by going when try peptide drive up died B a l o N. And losing is considered. It gives the information that Arnie Pain has failing and loosen on it either side from the earlier assumption. It is a zit is clear that our anything has followed by Listen, we can say that Berlin is present before Arnie Tim again. If we consider the try peptide Mellen, our 10. Do you see? It is being clear that the peptides are being repeated. So by all the verb your girlfriend says, we can say that have died. You know? President 20 obtained from Vassily based Sillas Breakfast, which is and the verdict up Days Properties. It's a sigh. Click only Go peptide that is the core peptide with this Chuck Chuck. Thus we can say well in followed by or Nathan followed by Loosen, followed by finial. Elhanan Fallen that by pro lead, followed by Vallin again. Then again, are Norton, followed by losing, followed by finial 11, Fathered by Problem, then again.

This question that we're looking at an experiment on kindness in walking along a micro to bill and actual questions are quite easy. It's really understanding the experiment that's been done. That is the difficult part. So in vitro, what they've done is they've used a laser but exerts a force on a motor protein. So they use this laser to surround a motor protein and move it at their will, and they use this to attach it to a microbial. And then there's at present in the solution. So the constant as access to a T P. And they use this laser to push against the constant as it moves along. Democratie real Um, and the whole time there's a silica beads attached to the Paterson Sutent rocket and between the bead and the laser, the constant moving quite slowly, as if it were actually carrying a load along the microbial. So that's the experiment. Have questions or sub A we're looking at. We're looking at the picture of the textbook, which shows to kind of see molecules walking along our microbial, and it shows where they are as time passes soon. First of all, they are moving only in one direction towards the plus end of microbial. What supplies the energy required for this all that is at P hydro. Sis, When we hide relies ATP, The the kind of sin, uh, head undergoes a conformational change that causes for motor to move along the microbial. Uh huh B. So for me, we're looking at the average rate of movement of each kind of sin. So we have to kind of since one and two. So one, if we have look, it has moved 80 nanometers and it has taken about nine seconds. So 80 nanometers in nine seconds gives us a rate of, let's say, roughly 99 m per second. And if we have a look at two two has moved 80 nanometers as well, but it's done it in only five seconds. So it's 80/5. So this one is moving at 16 9 m per second. Um, so one thing to note is this is very, very slow. In vivo, it moves perhaps 100 times faster than this. But with the laser and the silica p, they're moving far, far slower, so that we can more easily tracked them. See what is the length of each step. So again, we've moved 80 nanometers in both cases, and if we count the number of steps we see each taking 10 steps. So for both kind of molecules, the average step is eight nanometers in length, 89 pieces. D We're exploring why it's eight nanometers eat. So we know that kind of sin binds to beta turbulence, and it stays on the same pro to filament and in each protein filaments for beta turbulence. Subunit repeats at eight nanometer intervals. So what might be happening here? Well, indicating that become Simosa is attaching to the beta table. Um, and for a step, what it does is the other, um so one of the globular domains stays attacked to the subunit, and the other one swings forward to attach the next one. So if you imagine some stepping stones, you have 1 ft on the stone, you're on and the second swings forward, and then you attach to the next stone and your back foot swings forward. So it's a lot like stepping service, so it's stepping from one beta turbulence subunits so next, while of the front of the main, because it so back, back. Popular domain swings forward. Finally, E. Is there any data that can tell us how many ATP modules are hydrolyzed per step? So we're looking for traces, and we're thinking, Is there anything that tells us how much 80 p we need? But we don't We don't know the 80 p concentration, and we also don't see any variety in the steps were very clean. It's just one after the other, without any any time between them. So hypothetically. If there were, if there was time between the steps, we could have a region where there's just not enough 80 p. Yes, it took, say, one ATP for multiple steps. Then we would expect the steps to come in clumps with time between them. So that's 11 possibility. However, there is no time between any of these, so there's just not enough data to tell us anything. So the answer here is just just No. If we if we wanted to know about how much a teepee was required that step we would need, um, we would need times where there wasn't enough ATP to perform a step, and there's none of that at every point. It tries to form a step. It succeeds, so it has more than enough. 80 p


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