| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7605658 | International Journal of Mass Spectrometry | 2013 | 11 Pages |
Abstract
⺠We examine the effect of sodium iodide on three model proteins using nESI-IM-MS. ⺠The number of iodides correlates to the number of available basic sites. ⺠The conformational space occupied by each protein is altered due to the presence of salt and columbic effects. ⺠Thermally induced unfolding is lessened in the presence of adducted iodide. ⺠Proteins have lower collision cross sections at 300 K than at 260 K.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Yana Berezovskaya, Massimiliano Porrini, Perdita E. Barran,