Surface hydrophobic clusters modulate the folding stability and molecular recognition of the disintegrin jarastatin.

ABSTRACT: Disintegrins are cysteine-rich proteins found in snake venoms. These proteins selectively bind to integrins, which play a key role in the regulation of many physiopathological processes. They are coreless proteins that display almost all hydrophobic residues on the protein surface. The exposed hydrophobic residues form surface clusters stabilized by the interaction with the hydrophilic residues in the vicinity and the hydration shell. In the present work, we aimed to determine the stability of surface hydrophobic clusters (SHCs) and their role in protein folding and biological activity. We used urea denaturation curves followed by ¹H and ¹⁵N chemical shifts to determine the free energy of unfolding (ΔG_F-U) and CLEANEX experiments to measure the water exchan

SUBMITTER: Vasconcelos AA 

PROVIDER: S-EPMC11930076 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature