Solution conformation of a heptadecapeptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coli. Combined use of 1H nuclear magnetic resonance and restrained molecular dynamics

J Mol Biol. 1985 Nov 20;186(2):435-55. doi: 10.1016/0022-2836(85)90116-0.


A nuclear magnetic resonance study on a heptadecamer (17-mer) peptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coli is presented under solution conditions (viz. 40% (v/v) trifluorethanol) where it adopts an ordered helical structure as judged by circular dichroism. Using a combination of two-dimensional nuclear magnetic resonance techniques, complete resonance assignments are obtained in a sequential manner. From the two-dimensional nuclear Overhauser enhancement spectra, a set of 87 approximate distance restraints is derived and used as the basis for three-dimensional structure determination with a restrained molecular dynamics algorithm in which the interproton distances are incorporated into the total energy function of the system in the form of an additional effective potential term. The convergence properties of this approach are tested by starting from three different initial structures, namely an alpha-helix, a beta-strand and a 3-10 helix. In all three cases, convergence to an alpha-helical structure is achieved with a root mean square difference of less than 3 A for all atoms and less than 2 A for the backbone atoms.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Circular Dichroism
  • DNA-Binding Proteins*
  • Escherichia coli / genetics
  • Escherichia coli Proteins
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Protein Conformation
  • Receptors, Cyclic AMP*
  • Solutions
  • Thermodynamics


  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • Receptors, Cyclic AMP
  • Solutions
  • cyclic AMP receptor protein, E coli