Stabilizing Effect of Zn2+ in Native Bovine Rhodopsin.
From: Department of Pharmacology, Case Western Reserve University, Cleveland, Ohio 44106, USA. paul.park@case.edu
The Journal of biological chemistry
- Publish Date: Apr 2007
- ISSN: 0021-9258
- Volume: 282
- Issue: 15
- Pages: 11377-85
- Medium: Print
- Language: English
- Citation (JAMA): Park Paul S-H, Sapra K Tanuj, Koliński Michał, et al. Stabilizing Effect of Zn2+ in Native Bovine Rhodopsin.. J. Biol. Chem. Apr 2007;282:11377-85
Abstract
Single-molecule force spectroscopy (SMFS) is a powerful tool to dissect molecular interactions that govern the stability and function of proteins. We applied SMFS to understand the effect of Zn2+ on the molecular interactions underlying the structure of rhodopsin. Force-distance curves obtained from SMFS assays revealed the strength and location of molecular interactions that stabilize structural segments within this receptor. The inclusion of ZnCl2 in SMFS assay buffer increased the stability of most structural segments. This effect was not mimicked by CaCl2, CdCl2, or CoCl2. Thus, Zn2+ stabilizes the structure of rhodopsin in a specific manner.
Mesh Headings (Keywords): Amino Acid Sequence, Animals, Cations, Divalent, Cattle, Cysteine, Disulfides, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Denaturation, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Rhodopsin, Rod Outer Segments, Spectrum Analysis, Zinc
Check for Full Text / PubMed Unique Identifier (PMID): 17303564
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