Characterization of a Fast Voltage-Sensing Protein using Voltage-Clamp Fluorometry
نویسندگان
چکیده
منابع مشابه
Voltage-dependent conformational changes in human Ca(2+)- and voltage-activated K(+) channel, revealed by voltage-clamp fluorometry.
Large conductance voltage- and Ca(2+)-activated K(+) (BK(Ca)) channels regulate important physiological processes such as neurotransmitter release and vascular tone. BK(Ca) channels possess a voltage sensor mainly represented by the S4 transmembrane domain. Changes in membrane potential displace the voltage sensor, producing a conformational change that leads to channel opening. By site-directe...
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در طی سالهای اخیراستفاده ازمنابع انرژی تجدید پذیر در شبکه های مدرن بنا به دلایل زیست محیطی و اقتصادی به طور گسترده استفاده شده است همچون نیروگاههای بادی و خورشیدی .ولتاژتولیدی این نیروگاهها اغلب به فرم dc می باشد وادوات الکترونیک قدرت به عنوان مبدل و پل بین شکل موج dc وac استفاده می شوند.این پروسه باعث ایجاد پالسهایی برروی شکل موج خروجی می شود که می تواند وارد تجهیزات قدرت همچون ترانسفورماتور ی...
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The voltage-clamp electrophysiology method is the gold standard for measuring the function of ion channels. In the past, this technique has had limited applicability in pharmaceutical drug discovery because of its low throughput, steep learning curve, and challenges in standardization of the experiments. Recently, new electrophysiology platforms have been developed, which are based on the use o...
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Much of what we know about the properties of ion channels in cell membranes has come from experiments using voltage clamp. In general, the method allows ion flow across a cell membrane to be measured as electric current, whilst the membrane voltage is held under experimental control with a feedback amplifier. The method was first developed by Cole (1949) and Hodgkin et al. (1952) for use with t...
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In the human sodium glucose cotransporter (hSGLT1) cycle, the protein undergoes conformational changes where the sugar-binding site alternatively faces the external and internal surfaces. Functional site-directed fluorometry was used to probe the conformational changes at the sugar-binding site. Residues (Y290, T287, H83, and N78) were mutated to cysteines. The mutants were expressed in Xenopus...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2016
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2015.11.613