Abstract
Among molecular recognition systems, hinge-motion binding proteins (HMBPs) demonstrate exquisite selectivity toward their corresponding ligand or analyte, with affinities down to the nanomolar range. Elizabeth A. Moschou, Leonidas G. Bachas, and Sylvia Daunert at the University of Kentucky and Sapna K. Deo at Indiana University-Purdue University Indianapolis focus on calmodulin and one class of HMBPs, the periplasmic binding proteins.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 6692-6700 |
| Number of pages | 9 |
| Journal | Analytical Chemistry |
| Volume | 78 |
| Issue number | 19 |
| DOIs | |
| State | Published - Oct 1 2006 |
| Externally published | Yes |
ASJC Scopus subject areas
- Analytical Chemistry
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Cite this
Moschou, E. A., Bachas, L. G., Daunert, S., & Deo, S. K. (2006). Hinge-motion binding proteins: Unraveling their analytical potential. Analytical Chemistry, 78(19), 6692-6700. https://doi.org/10.1021/ac069464r