Can molecular confinement alter protein structure and stability? This study explores the use of sol-gel encapsulation in a silica matrix to investigate the effects of molecular confinement on proteins. Silica entrapment proves compatible with structure analysis by circular dichroism, allowing conformational studies in solvents that promote aggregation. The findings indicate that encapsulation generally enhances thermal protein stability. Lysozyme, α-lactalbumin, and metmyoglobin retain native-like structures, while apomyoglobin is largely unfolded. The addition of neutral salts influences encapsulated apomyoglobin's α-helical content, aligning with the Hofmeister ion series. The study proposes that protein conformation is influenced by confined water properties within the silica pores, offering valuable insights into protein behavior under constrained conditions.
Published in Protein Science, this research aligns with the journal’s focus on protein structure, function, and stability. The study’s investigation of molecular confinement effects on protein conformation complements existing research in the journal on protein folding, dynamics, and interactions.
| Category | Category Repetition |
|---|---|
| Science: Chemistry | 159 |
| Science: Biology (General) | 109 |
| Science: Chemistry: Organic chemistry: Biochemistry | 92 |
| Science: Chemistry: Physical and theoretical chemistry | 89 |
| Science: Physics | 74 |