AI Article Synopsis
- The study focused on how the protein annexin VI (AnxVI) folds in acidic conditions to understand its role in forming ion channels in membranes.
- Using a specific hydrophobic probe, researchers found that AnxVI exhibits a notable increase in hydrophobicity at low pH levels.
- Circular dichroism analysis showed that acidic pH causes AnxVI to lose its alpha-helical structure and develop new beta-structures, changes that can revert back when pH increases, suggesting a mechanism for the protein's ability to interact with membranes.
Article Abstract
Acidic pH-induced folding of annexin (Anx)VI in solution was investigated in order to study the mechanism of formation of ion channels by the protein in membranes. Using 2-(p-toluidino)naphthalene-6-sulfonic acid as a hydrophobic probe, it was demonstrated that AnxVI exerts a large change in hydrophobicity at acidic pH. Moreover, circular dichroism spectra indicated that the native state of AnxVI changes at acidic pH towards a state characterized by a significant loss of alpha-helix content and appearance of new beta-structures. These changes are reversible upon an increase of pH. It is postulated that the structural folding of AnxVI could explain how a soluble protein may undergo transition into a molecule able to penetrate the membrane hydrophobic region. The physiological significance of these observations is discussed.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/s0014-5793(01)02402-4 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!