Fluorescence studies of protein thermostability in ionic liquids

文献信息

发布日期 2004-03-19
DOI 10.1039/B401304M
影响因子 6.222
作者

Sheila N. Baker, T. Mark McCleskey, Siddharth Pandey, Gary A. Baker


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摘要

Using the single tryptophan residue in the sweet protein monellin as a spectroscopic handle, we show the extreme thermodynamic stabilization offered by an ionic liquid; Tun ∼ 105 °C in [C4mpy][Tf2N] compared to 40 °C in bulk water.

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来源期刊

Chemical Communications

Chemical Communications
CiteScore: 8.6
自引率: 4.7%
年发文量: 2458

ChemComm publishes urgent research which is of outstanding significance and interest to experts in the field, while also appealing to the journal’s broad chemistry readership. Our communication format is ideally suited to short, urgent studies that are of such importance that they require accelerated publication. Our scope covers all topics in chemistry, and research at the interface of chemistry and other disciplines (such as materials science, nanoscience, physics, engineering and biology) where there is a significant novelty in the chemistry aspects. Major topic areas covered include: Analytical Chemistry Catalysis Chemical Biology and medicinal chemistry Computational Chemistry and Machine Learning Energy and sustainable chemistry Environmental Chemistry Green Chemistry Inorganic Chemistry Materials Chemistry Nanoscience Organic Chemistry Physical Chemistry Polymer Chemistry Supramolecular Chemistry

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