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An Insight into the pathway of the amyloid fibril formation of hen egg white lysozyme obtained from a small-angle X-ray and neutron scattering study.
It is known that hen egg white lysozyme (HEWL) forms amyloid fibrils. Since HEWL is one of the proteins that have been studied most extensively and is closely related to human lysozyme, the variantsExpand
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Enthalpic destabilization of a mutant human lysozyme lacking a disulfide bridge between cysteine-77 and cysteine-95.
To understand the role of disulfide bridges in protein stability, the thermodynamic changes in the denaturation of two mutant human lysozymes lacking a disulfide bridge between Cys-77 and Cys-95Expand
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Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit.
To elucidate the role of individual amino acid residues in stabilizing the conformation of a protein, we have constructed a series of variant alpha subunits of tryptophan synthase from EscherichiaExpand
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Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution
  • S. Goda, K. Takano, +5 authors K. Namba
  • Chemistry, Medicine
  • Protein science : a publication of the Protein…
  • 31 December 2008
Mutant human lysozymes (Ile56Thr & Asp67His) have been reported to form amyloid deposits in the viscera. From the standpoint of understanding the mechanism of amyloid formation, we searched forExpand
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Contribution of water molecules in the interior of a protein to the conformational stability.
Water molecules frequently occur in the interior of globular proteins. To elucidate the contribution of buried water molecules to the conformational stability of a protein, we examined the crystalExpand
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Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,).
In globular proteins, there are intermolecular hydrogen bonds between protein and water molecules, and between water molecules, which are bound with the proteins, in addition to intramolecularExpand
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A new scale for side-chain contribution to protein stability based on the empirical stability analysis of mutant proteins.
The hydrophobicity scales for amino acid side chains based on the transfer Gibbs energy (DeltaG(trans)) of amino acids from non-aqueous phases to water have been widely used to estimate theExpand
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Structure and implications for the thermal stability of phosphopantetheine adenylyltransferase from Thermus thermophilus.
Phosphopantetheine adenylyltransferase (PPAT) is an essential enzyme in bacteria that catalyzes the rate-limiting step in coenzyme A (CoA) biosynthesis by transferring an adenylyl group from ATP toExpand
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Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants.
In order to understand the contribution of hydrophobic residues to the conformational stability of human lysozyme, five Ile mutants (Ile --> Val) in the interior of the protein were constructed. TheExpand
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Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus.
The structure of methionine aminopeptidase from hyperthermophile Pyrococcus furiosus (PfMAP) with an optimal growth temperature of 100 degreesC was determined by the multiple isomorphous replacementExpand
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