Re: Helix Native Mac Download
Atila Kalina
I'm trying to use a Chocolate Midi Foot Controller to change the SnapShots in Helix Native. The good news is (after following a Youtube video very closely) I got the pedals to change the snapshots. The bad news is I've got no sound! Argh! If I just put in a regular audio track and turn on "Input Echo" the sound plays through me UR22 Audio Interface and sounds great, but when I do the "split instrument track" setting (so I can use the foot switches) no sound comes out. Please help!
It seems like I must have something wrong with it going from the UR22, but I'm not sure what, or where I would change that. Either that, or I'm just missing a simple step in Cakewalk. Anyway, if anyone has any thoughts, I'd really appreciate it. I spent all day trying to solve this and got nowhere.
From what I can tell, the ONLY thing I'm doing differently than the Youtube video is that they are using bluetooth for their controller and I'm using a USB cable. Since the switches are doing what they are supposed to, I'm assuming that isn't the problem. Thanks again!!!
I don't think you want to create an instrument track for Helix native. It is an effect not a source of audio. You would create an audio track, record some audio, like a guitar, then add helix as an effect in the effect bin,
That's what I though initially, but when I tried doing it that way, it wouldn't let me control the Snapshots correctly. When I researched how to do this in various DAWS, several sources talked about creating a midi track and then routing it through the audio track (which is completely new to me). . When I researched how to do this in Cakewalk, I came across the video that I mentioned.
Following the video's instructions, it just seems like there is no audio input from an audio interface in the chain at all. I feel like I'm either not understanding something, or the directions are a little off.
For amp modelers you add them as fx on an audio track. If you want to use a midi controller you need to add a midi track. In the Helix native plugin enable midi input. The input on the midi track will be the midi controller and set the output to Helix native.
However constantly mull the idea of getting a Surface Pro to run HELIX Native on via Ableton. I use Ableton a lot anyway so to be able to use both on tablet live would be cool.
Maybe while also using an iPad. In addition there is now a Windows 10 version of Touchable Pro which can run on a surface tablet so one can control Ableton on windows tablets ( along with helix Native hosted inside ) using a touch centric control surface, touchable, like already exists and is highly lauded on iOS.
For owners of HELIX Hardware units HELIX NATIVE provides just more ways to use ones presets and for studio use etc can be very practical. Just make sure you use s top notch guitar interface like apogee.
presets aren't shared so much in the FB group itself but many of the videos of people showing off their playing with HELIX presets do share the presets use - either directly or via some cloud method - or very often like you say CustomTone.
I had the floor units and Native. It's perhaps strange, but I like Native more that the identical hardware. Has something to do with the Audio interface. You have more options with Native. The hardware unit's have a variable input impedance but it's limited, and didn't work all that well with my pickups.
I am making a preset in mainstage to control the snapshot of helix Native, everything is in order and working, but I would like to know if you have any idea to configure the MC6 PRO so that when selecting one of the switch can be seen as on, something similar to this example that I did with a Neural plug in where it is easy with the toggle option but in helix native the snapshot are called by Snapshot index and it is only necessary 1 message CC with value 127, and in Neural you can use the toggle function to use CC 0 to turn off and CC 127 to turn on and each one can be assigned a different color to differentiate when it is on or off.
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Antibody probing of Western blots is a method for analyzing the apparent Mr of a protein in any given preparation (Renart, J., Reiser, J., and Stark, G., Proc. Natl. Acad. Sci. USA 76: 3116, 1979). We prepared a rabbit antiserum to purified mouse myeloma helix destabilizing protein-1 and used this antiserum in Western blotting experiments with a crude homogenate of mouse myeloma. The results indicated that the native species of helix destabilizing protein-1 can be degraded during purification. This in vitro proteolysis results in complete loss of the native species and accumulation of lower Mr proteins that represent limit digestion products. These findings have identified the true native form of mouse myeloma HDP-1 as a protein of apparent Mr = 36,000 to 38,000, instead of the Mr = 24,000 and 27,000 proteins obtained by routine purification.
The native and the molten globule states (N and MG states, respectively) of canine milk lysozyme (CML) were examined by CD spectroscopy and AGADIR algorithm, a helix-coil transition program. It revealed that the helical content of the MG state was higher than that of the N-state, suggesting that non-native α-helix is formed in the MG state of CML. Using AGADIR, it indicated the possibility of α-helix formation in the third β-strand region in the MG state. To investigate this possibility, we designed a mutant, Q58P, in which the helical propensity of the MG state was significantly decreased around the third β-strand region. It appeared that the absolute ellipticity value at 222 nm of the mutant in the MG state was smaller than that of the wild-type protein. It could be assumed that the non-native α-helix is formed around the third β-strand region of wild-type CML in the MG state.
N2 - Proteolysis has a critical role in transmitting information within a biological system and therefore an important element of biology is to determine the subset of proteins amenable to proteolysis. Until recently, it has been thought that proteases cleave native protein substrates only within solvent exposed loops, but recent evidence indicates that cleavage sites located within α-helices can also be cleaved by proteases, despite the conformation of this secondary structure being generally incompatible with binding into an active site of a protease. In this study, we address the mechanism by which a serine endopeptidase, thrombin, recognizes and cleaves a target sequence located within an α-helix. Thrombin was able to cleave a model substrate, protein G, within its α-helix when a suitable cleavage sequence for the enzyme was introduced into this region. However, structural data for the complex revealed that thrombin was not perturbing the structure of the α-helix, thus it was not destabilizing the helix in order to allow it to fit within its active site. This indicated that thrombin was only cleaving within the α-helix when it was in an unfolded state. In support of this, the introduction of destabilizing mutations within the protein increased the efficiency of cleavage by the enzyme. Our data suggest that a folded α-helix cannot be proteolytically cleaved by thrombin, but the species targeted are the unfolded conformations of the native state ensemble.
AB - Proteolysis has a critical role in transmitting information within a biological system and therefore an important element of biology is to determine the subset of proteins amenable to proteolysis. Until recently, it has been thought that proteases cleave native protein substrates only within solvent exposed loops, but recent evidence indicates that cleavage sites located within α-helices can also be cleaved by proteases, despite the conformation of this secondary structure being generally incompatible with binding into an active site of a protease. In this study, we address the mechanism by which a serine endopeptidase, thrombin, recognizes and cleaves a target sequence located within an α-helix. Thrombin was able to cleave a model substrate, protein G, within its α-helix when a suitable cleavage sequence for the enzyme was introduced into this region. However, structural data for the complex revealed that thrombin was not perturbing the structure of the α-helix, thus it was not destabilizing the helix in order to allow it to fit within its active site. This indicated that thrombin was only cleaving within the α-helix when it was in an unfolded state. In support of this, the introduction of destabilizing mutations within the protein increased the efficiency of cleavage by the enzyme. Our data suggest that a folded α-helix cannot be proteolytically cleaved by thrombin, but the species targeted are the unfolded conformations of the native state ensemble.
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