2024-03-29T07:42:13Zhttps://keep.lib.asu.edu/oai/requestoai:keep.lib.asu.edu:node-1355132021-08-11T21:09:57Zoai_pmh:all135513
https://hdl.handle.net/2286/R.I.37544
http://rightsstatements.org/vocab/InC/1.0/
2016-05
36 pages
eng
Canarie, Elizabeth Rose
Allen, James
Wolf, George
School of Mathematical and Statistical Sciences
School of Molecular Sciences
Barrett, The Honors College
Text
Circular Dichroism (CD) and electron paramagnetic resonance (EPR) were used to investigate the metal-binding sites of five different four-helix bundles, which have slight differences in the population of their side chains. Of the four-helix bundles, three have central dinuclear metal binding sites; two of these three also have outer dinuclear metal binding sites. The other two peptides have two identical, non-central, dinuclear metal binding sites. The CD spectra showed changes in the secondary structure of the peptides, and X-band EPR spectra of these peptides revealed the unique four peak signal of Cu(II). These findings improve our understanding of the metal binding environments of these peptides.
Electronic Structure
Physical Chemistry
Chemistry
Investigation of Cu(II) Binding Sites in de Novo Proteins by Electron Paramagnetic Resonance Spectroscopy