In pre-sterol carrier protein 2 (SCP2) in solution the leader peptide 1-20 is flexibly disordered, and residues 21-143 adopt the same globular fold as in mature SCP2

F. E. Weber, Jim Dyer, F. López García, M. Werder, T. Szyperski, K. Wüthrich, H. Hauser

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The preform of the rabbit sterol carrier protein 2 (pre-rSCP2) was cloned, the uniformly 15N-labelled protein expressed in Escherichia coli and studied by three-dimensional 15N-resolved nuclear magnetic resonance spectroscopy. In spite of its low solubility in aqueous solution of only ~ 0.3 mM, sequential 15N and 1H backbone resonance assignments were obtained for 105 out of the 143 residues. From comparison of the sequential and medium-range nuclear Overhauser effects (NOEs) in the two proteins, all regular secondary structures previously determined in mature human SCP2 (hSCP2) were also identified in pre-rSCP2. Near-identity of the backbone 15N and 1H chemical shifts and 1:1 correspondence of 24 long-range NOEs to backbone amide groups in the two proteins show that the residues 21-143 adopt the same globular fold in pre-rSCP2 and mature hSCP2. The N-terminal 20-residue leader peptide of pre-rSCP2 is flexibly disordered in solution and does not observably affect the conformation of the polypeptide segment 21-143.

Original languageEnglish
Pages (from-to)751-759
Number of pages9
JournalCellular and Molecular Life Sciences
Issue number7
StatePublished - 28 Aug 1998



  • N-terminal leader peptide
  • Nuclear magnetic resonance
  • Protein expression
  • Protein structure
  • Sterol carrier protein 2

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