Author/Authors :
Lantz، نويسنده , , Mark A. and Jarvis، نويسنده , , Suzanne P. and Tokumoto، نويسنده , , Hiroshi and Martynski، نويسنده , , Tomasz and Kusumi، نويسنده , , Toshinori and Nakamura، نويسنده , , Chikashi and Miyake، نويسنده , , Jun، نويسنده ,
Abstract :
Atomic force microscopy was used to measure the force required to stretch individual molecules of the peptide cysteine3–lysine30–cysteine from the α-helical state into a linear chain (approximately 200 pN). The measured force versus peptide elongation was used to calculate the work done in breaking the hydrogen bonds which give rise to the helical structure. The average experimental value of the hydrogen-bond energy (20.2 kJ/mol) is in good agreement with reported theoretical calculations. In addition, the stiffness of individual peptides was measured directly using a force modulation technique and found to vary from approximately 0.005–0.012 N/m during elongation.
