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Volumn 306, Issue 5695, 2004, Pages 491-495

Molecular architecture of the KvAP voltage-dependent K+ channel in a lipid bilayer

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; DATA ACQUISITION; PARAMAGNETIC RESONANCE;

EID: 5644258235     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1101373     Document Type: Article
Times cited : (200)

References (37)
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    • note
    • Starting with a cysteine-less construct of full-length KvAP, we generated 144 cysteine mutants across the entire sequence of the voltage-sensor domain (S1 to S4) and the C-terminal end of S6. Of these, 131 mutants yielded protein suitable for structural studies (>90% coverage), as determined from its oligomeric state in gel-filtration analysis (not shown). Individual mutants were expressed, spin labeled, and reconstituted in DOPC:DOPG lipid bilayers (3:1) and symmetric KCl solutions for spectroscope measurements.
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    • note
    • 2) is indicative of exposure to membrane lipids, residues exposed to the aqueous environment display high NiEdda accessibilities (ΠNiEdda).
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    • note
    • Materials and methods are available as supporting material on Science Online.
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    • note
    • + channel models and paddle model. D. Cooper kindly assisted in generating the movie file for the supporting online material. This work was supported in part by NIH.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.