Variation of linker length in ratiometric fluorescent sensor proteins allows rational tuning of Zn(II) affinity in the picomolar to femtomolar range

Journal of the American Chemical Society

Volumn 129, Issue 12, 2007, Pages 3494-3495

  Van Dongen, Elisabeth M W M ^a   Evers, Toon H ^a   Dekkers, Linda M ^a   Meijer, E W ^a   Klomp, Leo W J ^b   Merkx, Maarten ^a  

^a EINDHOVEN UNIVERSITY OF TECHNOLOGY   (Netherlands)

^b UNIVERSITY MEDICAL CENTER UTRECHT   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN DERIVATIVE; ZINC;

ARTICLE; BINDING AFFINITY; FLUORESCENCE; MOLECULAR SIZE; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN STRUCTURE; SENSOR; STRUCTURE ANALYSIS;

CROSS-LINKING REAGENTS; FLUORESCENCE RESONANCE ENERGY TRANSFER; MODELS, MOLECULAR; PEPTIDES; PROTEIN STRUCTURE, TERTIARY; PROTEINS; ZINC;

EID: 33947631807     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja069105d     Document Type: Article

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