Guanidinium-Induced Denaturation by Breaking of Salt Bridges
نویسندگان
چکیده
منابع مشابه
Protein Denaturation with Guanidinium: A 2D-IR Study
Guanidinium (Gdm+) is a widely used denaturant, but it is still largely unknown how it operates at the molecular level. In particular, the effect of guanidinium on the different types of secondary structure motifs of proteins is at present not clear. Here, we use two-dimensional infrared spectroscopy (2D-IR) to investigate changes in the secondary structure of two proteins with mainly α-helical...
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Dry molten globular (DMG) intermediates, an expanded form of the native protein with a dry core, have been observed during denaturant-induced unfolding of many proteins. These observations are counterintuitive because traditional models of chemical denaturation rely on changes in solvent-accessible surface area, and there is no notable change in solvent-accessible surface area during the format...
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Urea and GdmCl are widely used to denature proteins at high concentrations. Here, we used MD simulations to study the denaturation mechanisms of helical peptide in different concentrations of GdmCl and urea. It was found that the helical structure of the peptide in water simulation is disappeared after 5 ns while the helicity of the peptide is disappeared after 70 ns in 2 M urea and 25 ns in 1 ...
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Viscosity measurements in 6 M guanidinium chloride (Gdm.Cl) (pH 5.2, 25”) suggest that Kunitz soybean trypsin inhibitor (STI) undergoes a slow unfolding which requires over 2 weeks to reach completion. The reduced viscosity increased during this time from an initial value of 3.5 ml/g to a final value of 16 to 17 ml/g. At pH 7 and 25”, over 4 weeks were required to reach the same final state. Ge...
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The unfolding thermodynamics of the circular enterocin protein AS-48, produced by Enterococcus faecalis, has been studied. The native structure of the 70-amino-acid-long protein turned out to be extremely stable against heat and denaturant-induced unfolding. At pH 2.5 and low ionic strength, it denatures at 102 degrees C, while at 25 degrees C, the structure only unfolds in 6.3 M guanidinium hy...
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ژورنال
عنوان ژورنال: Angewandte Chemie International Edition
سال: 2015
ISSN: 1433-7851
DOI: 10.1002/anie.201508601