| Literature DB >> 17303564 |
Paul S-H Park1, K Tanuj Sapra, Michał Koliński, Sławomir Filipek, Krzysztof Palczewski, Daniel J Muller.
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.Entities:
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Year: 2007 PMID: 17303564 PMCID: PMC2043472 DOI: 10.1074/jbc.M610341200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157