Abstracts:
Atomic force microscopy was used to measure the force required
to stretch individual molecules of the peptide cysteine3-lysine30-cysteine
from the α-herical 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 herical structure. The average experimental
value of the hydrogen-bond energy (20.2kJ/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 0.005-0.012N/m
during elongation. |
●AFMによる分子間相互作用の解析
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