Bykov, S and Asher, S
(2010)
Raman studies of solution polyglycine conformations.
Journal of Physical Chemistry B, 114 (19).
6636 - 6641.
ISSN 1520-6106
![[img]](http://d-scholarship-dev.library.pitt.edu/style/images/fileicons/text_plain.png) |
Plain Text (licence)
Available under License : See the attached license file.
Download (1kB)
|
Abstract
Polyglycine (polygly) is an important model system for understanding the structural preferences of unfolded polypeptides in solution. We utilized UV resonance and visible Raman spectroscopy to investigate the conformational preferences of polygly peptides of different lengths in water containing LiCl and LiClO4. Lithium salts increase the solubility of polygly. Our study indicates that in solution the conformational ensemble of polygly, as well as central peptide bonds of gly5 and gly6, are dominated by the 31 extended helix, also known as the polyglycine II conformation (PGII). This preference of the polygly backbone for the PGII conformation in solution is likely a result of favorable interactions between carbonyl dipoles in these extended helices. We found that high concentrations of Li+ stabilize the PGII conformation in solution, most likely by polarizing the peptide bond carbonyls that makes PGII-stabilizing carbonyl-carbonyl electrostatic interactions more favorable. This ability of Li+ to stabilize 31-helix conformations in solution gives use to the denaturing ability of lithium salts. © 2010 American Chemical Society.
Share
| Citation/Export: |
|
| Social Networking: |
|
Details
Metrics
Monthly Views for the past 3 years
Plum Analytics
Altmetric.com
Actions (login required)
 |
View Item |
![[feed]](/images/feed-icon-32x32.png){kind=icon}