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  • Basic pancreatic trypsin inhibitor  (1)
  • Biochemistry  (1)
  • 1
    Book
    Book
    Prinzipien der Biochemie (1998)
    Heidelberg : Spektrum, Akad. Verl.
    Details Availability
    Keywords: Biochemistry ; Lehrbuch ; Biochemie ; Biochemie
    Description / Table of Contents: Klappentext: Mit dem "Lehninger" wuchs eine ganze Generation von Studenten auf. Seine außergewöhnliche Klarheit der Darstellung und die gute Lesbarkeit haben Maßstäbe gesetzt. Der Lehninger - der erfolgreiche Lehrbuchklassiker: Umfassend - durch die nahezu lückenlose Darstellung biochemischen Grundwissens Verständlich - durch die außergewöhnliche Klarheit der Sprache und die durchgehend vierfarbige Gestaltung Aktuell - durch vertiefende Exkurse aktueller Themen, in der deutschen Ausgabe nochmals erweitert.
    Type of Medium: Book
    Pages: XLVII, 1223 S. , zahlr. Ill., graph. Darst. , 28 cm
    Edition: 2. Aufl., Studienausg.
    ISBN: 3827403251
    Series Statement: Spektrum Lehrbuch
    Uniform Title: Principles of biochemistry 〈dt.〉
    URL: https://external.dandelon.com/download/attachments/dandelon/ids/DE00411079368ADF309AEC125775900449A81.pdf
    RVK:
    WD 4000
    RVK:
    WD 4010
    Language: German
    Note: Literaturangaben , Literaturangaben
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  • 2
    Electronic Resource
    Electronic Resource
    1H NMR studies at 360 Mhz of the methyl groups in native and chemically modified basic pancreatic trypsin inhibitor (BPTI) (1977)
    Springer
    European biophysics journal 3 (1977), S. 303-315 
    Details
    ISSN: 1432-1017
    Keywords: NMR ; Proteinase inhibitor ; Protein modification ; Protein structure ; Basic pancreatic trypsin inhibitor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract In the 1H NMR spectra obtained at 360 MHz after digital resolution enhancement, the multiplet resonances of the methyl groups in the basic pancreatic trypsin inhibitor (BPTI) were resolved. With suitable double irradiation techniques the individual methyl resonances were assigned to the different types of aliphatic amino acid residues. Furthermore, from pH titration and comparison of the native protein with chemically modified BPTI, the resonance lines of Ala 16 in the active site and Ala 58 at the C-terminus were identified. Potential applications of the resolved methyl resonances as natural NMR probes for studies of the molecular conformations are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00535703
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    Paper (German National Licenses)
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