Published: 11 March, 2020 | Volume 4 - Issue 1 | Pages: 009-019
Figure 9:
Helical conformation of α - peptide at the stationary state is illustrated by (red dotted line), which has pitch height 5.4Ao, and radius 6Ao and 3 rings. When it is exposed to the spontaneous relaxation under the positive interfacial Gibbs free energy of gs = +500 erg/cm2 [= 1.677GPa] under 1 ATM pressure (isobaric) then the unfolding takes place (blue line), which is found to be 86.4% of the full transition, having Θ = 3.077 cycle.
Read Full Article HTML DOI: 10.29328/journal.abse.1001008 Cite this Article Read Full Article PDF
HSPI: We're glad you're here. Please click "create a new Query" if you are a new visitor to our website and need further information from us.
If you are already a member of our network and need to keep track of any developments regarding a question you have already submitted, click "take me to my Query."