4.6 Article

Stabilizing effect of Zn2+ in native bovine rhodopsin

Journal

JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 282, Issue 15, Pages 11377-11385

Publisher

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M610341200

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Funding

  1. NEI NIH HHS [K99 EY018085, EY08061, R00 EY018085-03, R01 EY008061, K99 EY018085-01, R01 EY008061-21, K99 EY018085-02, R00 EY018085, R00 EY018085-04, R00 EY018085-05] Funding Source: Medline

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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 inSMFSassay 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.

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