title: Stabilizing effect of Zn2+ in native bovine rhodopsin.
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.
authors.affiliation: Department of Pharmacology, Case Western Reserve University, Cleveland, Ohio 44106, USA. paul.park@case.edu
authors.forename: Paul S-H
authors.initials: PS
authors.lastname: Park
authors.forename: K Tanuj
authors.initials: KT
authors.lastname: Sapra
authors.forename: Michał
authors.initials: M
authors.lastname: Koliński
authors.forename: Sławomir
authors.initials: S
authors.lastname: Filipek
authors.forename: Krzysztof
authors.initials: K
authors.lastname: Palczewski
authors.forename: Daniel J
authors.initials: DJ
authors.lastname: Muller
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002413:Cations, Divalent / Q000737:chemistry; D002417:Cattle; D003545:Cysteine / Q000378:metabolism; D004220:Disulfides / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012243:Rhodopsin / Q000737:chemistry* / Q000378:metabolism*; D012374:Rod Cell Outer Segment / Q000378:metabolism; D013057:Spectrum Analysis; D015032:Zinc / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D002413:Cations, Divalent; D004220:Disulfides; D012243:Rhodopsin; D015032:Zinc; D003545:Cysteine