4.8 Article

Protein Salting Out Observed at an Air-Water Interface

Journal

JOURNAL OF PHYSICAL CHEMISTRY LETTERS
Volume 2, Issue 9, Pages 995-999

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jz200111q

Keywords

-

Funding

  1. Shiseido Female Researcher Science Grant
  2. Ministry of Education, Culture, Sports, Science and Technology of Japan [22018028]
  3. Grants-in-Aid for Scientific Research [22018028] Funding Source: KAKEN

Ask authors/readers for more resources

A protein salting-out process is directly observed at an air-water interface. By using time-resolved X-ray specular reflectivity and off-specular diffuse scattering, we identified several key stages in the adsorption of hen egg white lysozyme in a concentrated NaCl solution, (1) adsorption-induced unfolding, (2) monolayer formation with unfolded proteins, (3) protein refolding, and (4) island formation with the refolded proteins. Stages 3 and 4 are not observed either at the isoelectric point or in the salt-free solution, suggesting that they are induced by screening of the positive charges in the lysozyme by chloride ions. It is considered that the hydrated salt ions act to minimize the water-accessible surface area of the protein, not only enhancing protein dehydration (stages 1 and 2) but also assisting in protein refolding and association (stages 3 and 4). These results provide insight into the early stages of protein crystal nucleation.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.8
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available