Abstract
Arginine hydrochloride has been used to suppress protein aggregation during refolding and in various other applications. We investigated the structure of hen egg-white lysozyme (HEL) and solvent molecules in arginine hydrochloride solution by X-ray crystallography. Neither the backbone nor side-chain structure of HEL was altered by the presence of arginine hydrochloride. In addition, no stably bound arginine molecules were observed. The number of hydration water molecules, however, changed with the arginine hydrochloride concentration. We suggest that arginine hydrochloride suppresses protein aggregation by altering the hydration structure and the transient binding of arginine molecules that could not be observed.
| Original language | English |
|---|---|
| Pages (from-to) | 105-109 |
| Number of pages | 5 |
| Journal | Biophysical Chemistry |
| Volume | 137 |
| Issue number | 2-3 |
| DOIs | |
| Publication status | Published - 2008 Oct 1 |
| Externally published | Yes |
Keywords
- Arginine hydrochloride
- Crystal structure
- Hydration water molecules
- Lysozyme
- Protein aggregation
- Refolding
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Organic Chemistry
Fingerprint Dive into the research topics of 'Structure-based analysis reveals hydration changes induced by arginine hydrochloride'. Together they form a unique fingerprint.
Cite this
Nakakido, M., Tanaka, Y., Mitsuhori, M., Kudou, M., Ejima, D., Arakawa, T., & Tsumoto, K. (2008). Structure-based analysis reveals hydration changes induced by arginine hydrochloride. Biophysical Chemistry, 137(2-3), 105-109. https://doi.org/10.1016/j.bpc.2008.07.009