期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 130, 期 18, 页码 5836-+出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja7109037
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资金
- NCI NIH HHS [U54 CA119341, 1 U54 CA119341-01] Funding Source: Medline
- NIGMS NIH HHS [5 F32 GM077020, F32 GM077020, F32 GM077020-01] Funding Source: Medline
A plasmonic switch based on the calcium-induced conformational changes of calmodulin is shown to exhibit reversible wavelength modulations in response to changing calcium concentration. The extinction maximum (lambda(max)) of a localized surface plasmon resonance (LSPR) sensor functionalized with a novel calmodulin construct, cutinase-calmodulin-cutinase (CutCaMCut), reversibly shifts by 2-3 nm. A high-resolution (HR) LSPR spectrometer with a wavelength resolution (3 sigma) of 1.5 x 10(-2) nm was developed to detect these wavelength modulations in real-time, providing information about the dynamics and structure of the protein. The rate of conversion from open (Ca2+-bound) to closed (Ca2+-free) calmodulin is shown to be similar to 4-fold faster than the reverse process, with a closing rate of 0.127 s(-1) and opening rate of 0.034 s(-1). As far as we are aware, this plasmonic switch marks the first use of LSPR spectroscopy to detect reversible conformational changes in an unlabeled protein.
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