Generic high-capacity protein capture and release by pH control
نویسندگان
چکیده
منابع مشابه
Protein refolding by pH-triggered chaperone binding and release.
Molecular chaperones are typically either adenosine triphosphate (ATP) dependent or rely heavily on their ATP-dependent chaperone counterparts in order to promote protein folding. This presents a challenge to chaperones that are localized to ATP-deficient cellular compartments. Here we describe a mechanism by which the pH-regulated acid stress chaperone HdeA is capable of independently facilita...
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A hydrophilic macromolecular network is prepared by performing graft copolymerization of poly (sodium acrylate) chains onto salep and silica gel. The reaction parameters affecting the water absorbency of the superabsorbent composite were optimized using Taguchi method. FT-IR spectroscopy and Thermo Gravimetric Analysis (TGA) were used for confirming the s...
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چکیده این پایان نامه به بررسی اثر سیم پیچ مغناطیسی و کاوه یِ خوشه گر با بسامد رادیویی بر هاله و بیرونگراییِ باریکه هایِ پیوسته و خوشه ایِ ذرات باردار در شتابدهنده های خطیِ یونی، پروتونی با جریان بالا می پردازد و راه حل هایی برای بهینه نگهداشتن این کمیتها ارایه می دهد. بیرونگرایی یکی از کمیتهای اساسی باریکه هایِ ذرات باردار در شتابدهنده ها است که تاثیر قابل توجهی بر قیمت، هزینه و کاراییِ هر شتابدهند...
Cleavable trifunctional biotin reagents for protein labelling, capture and release.
Trifunctional biotin reagents incorporating cleavable linkers are evaluated for their usage in protein enrichment. A linker based on the Dde protecting group leads to efficient release of protein targets under mild conditions. It additionally contains a masked trypsin cleavage site, which eliminates the majority of the tag during tryptic digestion.
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ژورنال
عنوان ژورنال: Chemical Communications
سال: 2020
ISSN: 1359-7345,1364-548X
DOI: 10.1039/d0cc01250e