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Sequence-specific h-1-NMR assignments and identification of slowly exchanging amide protons in murine epidermal growth-factor

Academic Article
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Overview

authors

  • Montelione, G. T.
  • Wuthrich, Kurt
  • Scheraga, Harold

publication date

  • March 1988

journal

  • Biochemistry  Journal

abstract

  • Proton nuclear magnetic resonance (1H NMR) assignments for the murine epidermal growth factor (mEGF) in aqueous solution were determined by using two-dimensional NMR at pH 3.1 and 28 degrees C. The assignments are complete for all backbone hydrogen atoms, with the exception of the N-terminal amino group, and for 46 of the 53 side chains. Among the additional seven amino acid residues, three have complete assignments for all but one side-chain proton, and between two and four protons are missing for the remaining four residues. The sequential assignments by nuclear Overhauser effect spectroscopy are consistent with the chemically determined amino acid sequence. The NMR data show that the conformations of both the Tyr3-Pro4 and Cys6-Pro7 peptide bonds are trans in the predominant solution structure. Proton-deuterium exchange rate constants were also measured for 13 slowly exchanging amide protons. The information presented here has been used elsewhere to determine the three-dimensional structure of mEGF in aqueous solution.

subject areas

  • Amides
  • Amino Acid Sequence
  • Animals
  • Epidermal Growth Factor
  • Hydrogen
  • Magnetic Resonance Spectroscopy
  • Mice
  • Protein Conformation
  • Protons
  • Submandibular Gland
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Identity

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi00406a064

PubMed ID

  • 2837287
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Additional Document Info

start page

  • 2235

end page

  • 2243

volume

  • 27

issue

  • 6

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