The proposal that ligand mediated conformational changes in the C-terminal region alters the ability of OrbS to interact with core RNAP has similarities to the regulation of some members of the ECF41 and ECF42 groups. The long C-terminal extension of ECF41 σ factors folds into a SnoaL-like domain which is likely to regulate the activity of the fused σ factor in response to the binding of a low molecular weight ligand (91). In the absence of ligand the SnoaL-like domain maintains the fused σ factor in a closed (inhibitory) conformation through interaction between the C-terminal region of the SnoaL-like domain and the σ2-σ4 interdomain linker (62,92). Thus, like CorE and CorE2, ligand binding would activate ECF41 σ factors, possibly by promoting the adoption of a more open conformation that permits productive interaction with core RNAP. ECF42 σ factors possess a long C-terminal extension that ends with a tetratricopeptide repeat (TPR) domain (93). TPR domains are implicated in protein-protein interactions (94). Interaction between the σ4 proximal region of the C-terminal extension and the second and third α-helices of the σ4 domain is required for ECF42 σ activity (92,95). It has been suggested that binding of a ligand (possibly another protein) to the TPR domain results in conformational changes in the σ4 proximal region of the C-terminal extension to suppress ECF42 σ factor activity, presumably by disrupting the interaction with the second and third α-helices of the σ4 domain (92). Thus, as for OrbS, ligand binding to ECF42 σ factors inhibits their activity. However, it is not yet clear whether ligand binding alters the ability of ECF42 σ factors to interact with core RNAP or to impair DNA recognition, or both. The proposal that Fe(II) binding at the C-terminal region of OrbS impairs binding to core RNAP, as suggested here, offers the advantage that molecules of RNAP are not taken out of commission by their recruitment to inactivated σ factors.
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I have been experiencing a problem with some of my helix patches. If i try to simulate an amp breaking with some boost plus a two or more reverb block, after playing it for 3 - 5 minutes I hear that the output of my headphones and/or speakers start cracking, like if there was a lot of static and then suddenly the sound cuts off completely. To "fix" this I have to exit the patch and then enter it again. The problem will still happen after a couple of minutes playing it.
Now none of this matches the cracking, static type of noise that you have described as the problem, but now it gets very weird. While typing this reply I was listening to my iTune playlist through the Helix and I had switched back to your patch so that I might check some of your amp and FX settings. Guess what? Yep, while typing, there was a loud crack through the monitors followed by total silence! It seems that just having the preset selected for a short time was enough for it to shut down my audio playback system with an heart stopping thud. Considering I had a quintuple Coronary Artery Bypass Graft operation a few years back it is something I can do without. O.K. I have now disconnected my Tannoys and am about to check out some of your settings.
These effects of ripple and hum are also noted on the helixhelp website where there is a link to an article about "The Strange Effects of AC Ripple on a Class AB Power Amp". One for the mad scientists to read I think.
After you unroll bed-in-a-box mattresses and cut the vacuum bag open, they'll immediately begin to inflate, so unbox them on your bed frame or near it. They're usually ready to go in a few hours, but most manufacturers recommend you give the mattress two days to fully inflate. The room may also smell a bit gassy at first, so crack a window; the smell tends to dissipate within a day.
Percy woke up on a lovely morning in his newly rebuilt house, made some eggs despite not being able to eat, and walked outside to enjoy breakfast on his front porch, only to be surrounded by ANINA helicopters and soldiers. Not wanting to ruin his chance at a normal life Percy agreed to go to ANINA max security prison with this realities version of the Crimson Hand. After a bit of banter on the way there met with some suprising laughs from the Crimson Hand, Percy arrived at the place he was so used to carpet bombing for fun. He was brought into a 'not that protected' room and questioned for a while about who the hell he was and how he killed the kaiju. Throughout most of the interview many of the people watching were questioning if Percy even was the guy who killed the kaiju, he responded with grunts to most of the questions he was asked and didn't seem threatening at all.
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NMR structural model. a HSQC NMR spectrum of WhiB1. Note the weak intensity and unusual chemical shifts for Cys66 and Cys60. Residues in the TEV tag have negative residue numbers. sc, side chain. b Structural model of WhiB1 calculated using NMR restraints. The chain is colored from blue at the N terminus to red at the C terminus. The structure shown starts at residue 1, and finishes at residue 84. The two arginine residues 73 and 74 in the C-terminal helix are predicted to interact with DNA. For clarity amino acid residues are indicated using the single letter code. c The environment of the WhiB1[4Fe-4S] cluster. The only side chains shown are the coordinating cysteine residues. The protein is displayed as a cartoon, except for the loop containing Gly61 and Gly62, which is shown as stick representations
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