Disulfide crosslinks to probe the structure and flexibility of a designed four-helix bundle protein

Protein Sci. 1994 Dec;3(12):2419-27. doi: 10.1002/pro.5560031225.


The introduction of disulfide crosslinks is a generally useful method by which to identify regions of a protein that are close together in space. Here we describe the use of disulfide crosslinks to investigate the structure and flexibility of a family of designed 4-helix bundle proteins. The results of these analyses lend support to our working model of the proteins' structure and suggest that the proteins have limited main-chain flexibility.

MeSH terms

  • Amino Acid Sequence
  • Chromatography, Gel
  • Circular Dichroism
  • Computer Simulation*
  • Cystine / chemistry*
  • Helix-Loop-Helix Motifs
  • Models, Molecular*
  • Molecular Sequence Data
  • Motion
  • Oxidation-Reduction
  • Peptides / chemical synthesis
  • Peptides / chemistry
  • Protein Conformation*
  • Protein Denaturation
  • Protein Engineering*
  • Protein Structure, Secondary*


  • Peptides
  • Cystine