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Amide proton-exchange in the alpha-amylase polypeptide inhibitor tendamistat studied by two-dimensional h-1 nuclear-magnetic-resonance

Academic Article
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Overview

authors

  • Qiwen, W.
  • Kline, A. D.
  • Wuthrich, Kurt

publication date

  • 1987

journal

  • Biochemistry  Journal

abstract

  • The individual amide proton exchange rates in Tendamistat at pH 3.0 and 50 degrees C were measured by using two-dimensional 1H nuclear magnetic resonance. Overall, it was found that the distribution of exchange rates along the sequence is dominated by the interstrand hydrogen bonds of the beta-sheet structures. The slowly exchanging protons in the core of the two beta-sheets were shown to exchange via an EX2 mechanism. Further analysis of the data indicates that different large-scale structure fluctuations are responsible for the exchange from the two beta-sheets, even though the three-dimensional structure of Tendamistat appears to consist of a single structural domain.

subject areas

  • Amides
  • Amino Acid Sequence
  • Hydrogen
  • Hydrogen-Ion Concentration
  • Magnetic Resonance Spectroscopy
  • Peptides
  • Protons
  • alpha-Amylases
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Identity

International Standard Serial Number (ISSN)

  • 0006-2960

PubMed ID

  • 2827730
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Additional Document Info

start page

  • 6488

end page

  • 6493

volume

  • 26

issue

  • 20

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