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  • 1
    Electronic Resource
    Electronic Resource
    Primary structure of C-terminal functional sites in ovine rhodopsin (1981)
    [s.l.] : Nature Publishing Group
    Nature 293 (1981), S. 314-316 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Ovine opsin consists of a single glycosylated polypeptide of apparent molecular weight (MW) 38,000 and constitutes about 90% of the protein contained in the rod photoreceptor membranes. The bulk of the protein is thoroughly embedded in the lipid bilayer, which accounts for the limited ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/293314a0
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Peptide ladder sequencing by mass spectrometry using a novel, volatile degradation reagent (1994)
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 8 (1994), S. 737-742 
    Details
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: A conceptually novel approach to protein sequencing involves the generation of ragged-end polypeptide chains followed by mass spectroscopic analysis of the resulting nested set of fragments. We report here on the synthesis and development of a volatile isothiocyanate (trifluoroethylisothiocyanate) that allows the identification of several consecutive residues starting with a few picomoles of peptide. The nested set of peptides is generated simply by adding equal aliquots of starting peptide each cycle and driving both the coupling and cleavage reactions to completion. No additional reagents are required to act as chain terminators and retention of the peptide terminal amine allows for subsequent modification with quaternary ammonium alkyl NHS esters to improve sensitivity. Complex washing procedures are not required each cycle, as reagents and by-products are efficiently removed under vacuum, eliminating extractive loss. Multiple peptide samples can be processed simultaneously, with each degradation cycle completed in 35-40 min. The inherent simplicity of the process should allow for easy automation and permit rapid processing of samples in parallel.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/rcm.1290080916
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    Paper (German National Licenses)
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