Kinetic Refolding Barrier of Guanidinium Chloride Denatured Goose δ-Crystallin Leads to Regular Aggregate Formation
نویسندگان
چکیده
منابع مشابه
Refolding of denatured and denatured/reduced lysozyme at high concentrations.
Refolding of proteins at high concentrations often results in aggregation. To gain insight into the molecular aspects of refolding and to improve the yield of active protein, we have studied the refolding of lysozyme either from its denatured state or from its denatured/reduced state. Refolding of denatured lysozyme, even at 1 mg/ml, yields fully active enzyme without aggregation. However, refo...
متن کاملCooperative Unfolding of Residual Structure in Heat Denatured Proteins by Urea and Guanidinium Chloride
The denatured states of proteins have always attracted our attention due to the fact that the denatured state is the only experimentally achievable state of a protein, which can be taken as initial reference state for considering the in vitro folding and defining the native protein stability. It is known that heat and guanidinium chloride (GdmCl) give structurally different states of RNase-A, l...
متن کاملManipulation of the observed kinetic phases in the refolding of denatured ferricytochromes c.
The refolding of guanidine hydrochloride-denatured horse heart ferricytochrome c at pH 7.0 and 23 degrees C occurs in three kinetic phases as observed by stopped flow measurements using changes in Soret absorbance or in tryptophan fluorescence. The three kinetic phases have time constants of 10 +/- 5 ms, 240 +/- 30 ms, and 13 +/- 3 s accounting for 15 +/- 5%, 70 +/- 5%, and 15 +/- 5% of the tot...
متن کاملThe interaction of Glu294 at the subunit interface is important for the activity and stability of goose δ-crystallin
PURPOSE delta-Crystallin is a soluble structural protein in found in avian eye lenses; it shares high amino acid sequence identity with argininosuccinate lyase. E294 is the only residue located at the double dimer interface and it performs hydrogen bonding with the active site residues of H160 and K323 in the neighboring and diagonal subunits, respectively. H160 is reported to play an important...
متن کاملKinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride.
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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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2007
ISSN: 0006-3495
DOI: 10.1529/biophysj.107.104604