Conformational behaviour of the TraM headpiece

J Pept Res. 1998 Mar;51(3):244-50. doi: 10.1111/j.1399-3011.1998.tb01222.x.

Abstract

The structure of the headpiece of the TraM protein was investigated in different solvents. The very first 22 amino acids which alternate in their hydrophilic and hydrophobic character formed a helical structure in the presence of a membrane mimetic. In water alone the structure was flexible with a small amount of helicity according to circular dichroism measurements, whereas a loop structure was observed in dimethyl sulphoxide.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Circular Dichroism
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Protein Conformation

Substances

  • Bacterial Proteins
  • TraM protein, bacterial