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Conformation of a t-cell stimulating peptide in aqueous-solution

Academic Article
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Overview

authors

  • Waltho, J. P.
  • Feher, V. A.
  • Lerner, Richard
  • Wright, Peter

publication date

  • July 1989

journal

  • FEBS Letters  Journal

abstract

  • Using two-dimensional NMR spectroscopy and circular dichroism spectroscopy it is demonstrated that a T cell stimulating peptide corresponding to residues 132-153 of sperm whale myoglobin populates helical conformations in aqueous solution. This finding is in accordance with proposals that immunodominant sites in T cell stimulating peptides have a high conformational propensity. The observation of secondary structure in aqueous solutions of this and other immunogenic peptides has important implications for initiation of protein folding.

subject areas

  • Amino Acid Sequence
  • Animals
  • Circular Dichroism
  • Magnetic Resonance Spectroscopy
  • Myoglobin
  • Peptides
  • Protein Conformation
  • Solutions
  • T-Lymphocytes
  • Whales
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Identity

International Standard Serial Number (ISSN)

  • 0014-5793

Digital Object Identifier (DOI)

  • 10.1016/0014-5793(89)80764-1

PubMed ID

  • 2787756
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Additional Document Info

start page

  • 400

end page

  • 404

volume

  • 250

issue

  • 2

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