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Mesoscopic irreversible thermodynamics of morphological evolution kinetics of helical conformation in bioproteins ‘DNA’ under the isothermal isobaric conditions

Tarik Omer Ogurtani* and Ersin Emre Oren

Published: 11 March, 2020 | Volume 4 - Issue 1 | Pages: 009-019

abse-aid1008-g010

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a) Perspective view: 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 negative interfacial Gibbs free energy of gs = -500 erg/cm2 [p = -1.677GPa uniaxial tension, isobaric] the unfolding takes place (blue line), which is found to be 99.9% of the full transition b) Top View: Partial unfolding appears as an arc segment (blue color) having Θ = 49.5o azimuthal angle with a torsional inclination angle of β = 2.563o. That should be zero if one takes final total pitch height as p = lo

Read Full Article HTML DOI: 10.29328/journal.abse.1001008 Cite this Article Read Full Article PDF

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