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  • 1
    Electronic Resource
    Electronic Resource
    A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing (1983)
    [s.l.] : Nature Publishing Group
    Nature 302 (1983), S. 718-721 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] To identify a clone for a particular protein by DNA sequencing, the nucleotide sequence of a cDNA clone encoding a portion of the protein sequence must be determined. We determined sequences of cDNA fragments isolated from a library of rabbit muscle cDNA cloned into Ml3 phage11. Before cloning, the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/302718a0
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Advances in gas chromatographic mass spectrometric protein sequencing. 3 - Automated interpretation of the mass spectra of the polyamino alcohol derivatives (1981)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 8 (1981), S. 70-77 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A computer program, PEPALG, has been developed to interpret data generated in a gas chromatographic mass spectrometric experiment on a complex mixture of N-α, (ω)-trifluoroethyl-O-trimethylsilyl polyamino alcohols derived from a mixture of oligopeptides. The program incorporates all the types of data available to the user, including amino acid composition of the original protein or polypeptide, gas chromatographic retention indices, partial sequence information and the characteristics of the N-α, (ω)-trifluoroethyl-O-trimethylsilyl polyamino alcohol mass spectra. PEPALG has been used extensively in the past three years and is capable of correctly identifying in less than one hour at least 90% of the peptide derivatives in a gas chromatographic mass spectrometric experiment which generates 300 mass spectra.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200080205
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Advances in gas chromatographic mass spectrometric protein sequencing. 1 - optimization of the derivatization chemistry (1981)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 8 (1981), S. 51-61 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The derivatization chemistry for conversion of mixtures of oligopeptides to the corresponding N-α, (ω)-trifluoroethyl-O-trimethylsilyl polyamino alcohols, the derivatives of choice for the sequencing of polypeptides by gas chromatographic mass spectrometry, has been optimized. The improvements have minimized undesirable side reactions and resulted in a five- to tenfold increase in sensitivity over previous methods employing either lithium aluminum deuteride or hexadeuterodiborane as the reducing agent. For derivatives of certain very polar peptides increases in yield have exceeded 100-fold. The procedure has been evaluated with mixtures of synthetic oligopeptides and used in the course of the determination of the amino acid sequence of the membrane protein bacteriorhodopsin, as well as other proteins.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200080203
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  • 4
    Electronic Resource
    Electronic Resource
    Advances in gas chromatographic mass spectrometric protein sequencing. 2 - Application to membrane proteins (1981)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 8 (1981), S. 62-69 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The primary structure of the integral membrane protein bacteriorhodopsin was determined by an efficient combination of gas chromatographic mass spectrometric techniques with the Edman degradation. This combination of methodologies circumvented many of the experimental difficulties associated with the insolubility of bacteriorhodopsin and its primary degradation fragments in aqueous buffers. Specifically, in the gas chromatographic mass spectrometric analysis of the cyanogen bromide peptides derived from bacteriorhodopsin, it has been possible to identify homoserine-containing peptides which served as a starting point for the construction of C-terminal sequences. In most cases this C-terminal sequence constructed from the gas chromatographic mass spectrometric peptides overlapped the N-terminal sequence derived in an Edman degradation experiment, thereby completing the structure of the fragment. Furthermore, the specific identification of methionine-containing peptides required to establish the order of the cyanogen bromide fragments was accomplished by direct analysis of the complex mixtures generated by partial hydrolysis of segments of the protein. These data made it possible to determine the sequence of a large portion of bacteriorhodopsin solely from cyanogen bromide cleavage, one of the few specific reactions compatible with the solubility properties of this hydrophobic protein. Finally, the gas chromatographic mass spectrometric sequence data have been used to assign or confirm amino acids where the Edman data was ambiguous. These gas chromatographic mass spectrometric techniques resulted in an efficient and reliable determination of the complete sequence of this membrane protein which is 248 amino acids long.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200080204
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