Native Instruments

There is so much to Reaktor that it is impossible to give a fair introduction in just a few paragraphs. The reader is highly recomended to look at Native Instrument s Web site for more information and tutorials (the Web site address can be found in the HTML document web-refs.htm, available in folder various, on the CD-ROM). 

Keep an eye on Native Instruments Web site for updated versions of their systems. 

I would like to express my gratitude to all contributors who have kindly provided the materials for the CD-ROM Richard Moore (University of California, San Diego), Robert Thompson (Georgia State University), Kenny McAlpine (University of Glasgow), Stephan Schmitt and Jake Mandell (Native Instruments), Nicolas Fournel (Synoptic), Karnataka Group, Dave Smith (Seer Systems), Aluizio Arcela (University of Brasilia), Xavier Rodet and Adrien Lefevre (Ircam), Trevor Wishart, Archer Endrich, Richard Dobson and Robert Fraser (CDP), Jacques Chareyron (University of Milan), Arun Chandra (University of Illinois),... 

A completely new method of determining siufaces arises from the enormous developments in electron microscopy. In contrast to the above-mentioned methods where the surfaces were calculated, molecular surfaces can be determined experimentally through new technologies such as electron cryomicroscopy [188]. Here, the molecular surface is limited by the resolution of the experimental instruments. Current methods can reach resolutions down to about 10 A, which allows the visualization of protein structures and secondary structure elements [189]. The advantage of this method is that it can be apphed to derive molecular structures of maaomolecules in the native state. 

At Bayer CropScience, the use of a stable isotope IS has become common practice to eliminate the effects of matrix suppression on instrument signals. The stable isotopes are synthesized by deuterium exchange reactions on authentic native standards or the... 

This chapter has reviewed the application of ROA to studies of unfolded proteins, an area of much current interest central to fundamental protein science and also to practical problems in areas as diverse as medicine and food science. Because the many discrete structure-sensitive bands present in protein ROA spectra, the technique provides a fresh perspective on the structure and behavior of unfolded proteins, and of unfolded sequences in proteins such as A-gliadin and prions which contain distinct structured and unstructured domains. It also provides new insight into the complexity of order in molten globule and reduced protein states, and of the more mobile sequences in fully folded proteins such as /1-lactoglobulin. With the promise of commercial ROA instruments becoming available in the near future, ROA should find many applications in protein science. Since many gene sequences code for natively unfolded proteins in addition to those coding for proteins with well-defined tertiary folds, both of which are equally accessible to ROA studies, ROA should find wide application in structural proteomics. 

Figure 6. Fluorescence decay profiles of trans-7,8-dihydroxy-7,8-dihydro-BP and 8,9,10,11-tetrahydro-BA measured at 23 °C with and without native DNA. Taken from refs. 14 and 15. The upper left-hand corner contains an instrument response profile. Emission and excitation wavelengths, lifetimes, and values of x2 obtained from deconvolution of the lifetime data are also given.

Kuleff, I. and Pernicka, E. (1995). Instrumental neutron activation analysis of native copper - some methodological considerations. Journal of Radioanalytical and Nuclear... 

Figure 10.3 Whole-mass analysis of a monoclonal antibody. (A) Direct infusion of the antibody generates an envelope of high m/z ions ranging from 2000 to 3500. Deconvolution of the ion current signal gives the mass of the complete native molecule (147, 100.97 Da) and resolves some heterogeneity linked to the A-glycan structures. The major forms are consistent with molecules carrying biantennary structures capped with 0, 1, or 2 hexose (G = galactose) residues. (Data generated on an ESI-Q-Star instrument, Sciex-Applied Biosystems.)...

Because of its structural simplicity and instrumental role in protein function, the coiled coil is one of the most investigated protein folding motifs. Native coiled-coil sequences and their mutants have been synthesized and studied. Numerous model coiled-coil peptides have been designed de novo [22]. Although many theoretical questions remain unanswered, much has been learned about the sequence-structure relationship. It is even possible to design and engineer new coiled-coil sequences and structures that have never existed before [23]. 

Figure 5. Proton decoupled 19F-NMR spectrum of pABG5 / -glucosidase inactivated with 2F/ ManF (conditions as described in text). Spectra were recorded on a 270 MHz Bruker/Nicolet instrument using gated proton decoupling (decoupler on during acquisition only) and a 90° pulse angle with a repetition delay of 2s. A spectral width of 40,000 Hz was employed and signal accumulated over 10,000 transients for the native protein and 30,000 transients for the denatured protein in 8M urea, (a) Full spectrum with expansion below it (b) Expansion of spectrum of denatured/dialyzed enzyme.

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