Journal of Undergraduate Chemistry Research
Circular dichroism (CD) is an important structural biology technique used to study protein dynamics, and most especially the secondary structure of peptides and proteins. Although CD is a technique that is relatively easy to introduce to undergraduate students, the high cost of obtaining a conventional CD instrument and the time required for sample preparation prevents a good number of students from having hands-on experiments demonstrating the principle of CD. Herein, theoretical circular dichroism with the dipole interaction model, DInaMo, is proposed as a tool for introducing students to CD. Using the dipole interaction model, the CD spectra of an α-helical protein, calexcitin, is predicted with a good morphology, and peak intensity and location of the π– π* transition. The n–π* transition is well approximated with normal modes obtained in the correct location and sign.
Jungong, Akongnwi C.; Aleksandrov, Tsvetan; Nori, Rahul; Erickson, Justin; Thomasson, Kathryn A.; Uporov, Igor V.; Austhof, Ethan R.; Holt, Emily; and Ngassa, Felix N., "Theoretical Circular Dichroism Spectra of the α-Helical Protein Calexitin with the Dipole Interaction Model Including the n-π* Transition" (2018). Chemistry Faculty Publications. 23.