Time-dependent X-ray diffraction studies on urea/hen egg white lysozyme complexes reveal structural changes that indicate onset of denaturation

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Time-dependent X-ray diffraction studies on urea/hen egg white lysozyme complexes reveal structural changes that indicate onset of denaturation

Temporal binding of urea to lysozyme was examined using X-ray diffraction of single crystals of urea/lysozyme complexes prepared by soaking native lysozyme crystals in solutions containing 9 M urea. Four different soak times of 2, 4, 7 and 10 hours were used. The five crystal structures (including the native lysozyme), refined to 1.6 Å resolution, reveal that as the soaking time increased, more...

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X-ray Diffraction Studies on Crystalline Complexes

Complexes of the gene 5 protein with a variety of oligodeoxynucleotides, ranging in length from two to eight and having several different sequences, have been formed and crystallized for x-ray diffraction analysis. The crystallographic parameters of four different unit cells, all of which are based on hexagonal packing arrangements, indicate that the fundamental unit of the complex is composed ...

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DMSO-induced denaturation of hen egg white lysozyme.

We report on the size, shape, structure, and interactions of lysozyme in the ternary system lysozyme/DMSO/water at low protein concentrations. Three structural regimes have been identified, which we term the "folded" (0 < φ(DMSO) < 0.7), "unfolded" (0.7 ≤ φ(DMSO) < 0.9), and "partially collapsed" (0.9 ≤ φ(DMSO) < 1.0) regime. Lysozyme resides in a folded conformation with an average radius of g...

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Ultrafast structural changes measured by time-resolved X-ray diffraction

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To test the immunological prediction that there should be two amino acid sequence differences between the lysozymes of the bobwhite quail and the chicken, the sequences of these two lysozymes have now been compared. Lysozyme purified from bobwhite quail egg white was reduced, carboxymethylated, and digested with trypsin. The resulting 18 peptides were separated and their compositions determined...

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ژورنال

عنوان ژورنال: Scientific Reports

سال: 2016

ISSN: 2045-2322

DOI: 10.1038/srep32277