The conformation of an Éø helix in the scale of a single molecule in milliseconds was investigated by Atomic Force Microscopy

S. Takeda¹, A. Ptak¹, C. Nakamura¹, J. Miyake¹, M. Kageshima², S.P. Jarvis², H. Tokumoto²

1) National Institute for Advanced Industrial Science and Technology (AIST)
1-1-4 Higashi, Tsukuba, Ibaraki 305-8562, Japan
2) Joint Research Center for Atom Technology (JRCAT)
1-1-4 Higashi, Tsukuba, Ibaraki 305-8562, Japan

The conformations of peptides or proteins strongly dominate their properties. We investigated the conformation of the single helical peptide molecule using AFM by stretching the molecule with various speeds. In the force-extension curves, many rupturing points that seemed to be due to the breaking of some hydrogen bonds were observed and these points tended to disappear with decreasing the stretching speed. We will discuss about The conformation of an Éø helix in the scale of a single molecule in milliseconds.