• Publications
  • Influence
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 was found that under the monomer state the structural changes of HEWL were not gross changes in shape but local conformational changes, and the dimers, formed by the association at the end of the long axis of HewL, had an elongated shape. Expand
Enthalpic destabilization of a mutant human lysozyme lacking a disulfide bridge between cysteine-77 and cysteine-95.
Although X-ray crystallography indicated that the mutants preserve the wild-type tertiary structure, removal of the disulfide bridge increased the flexibility of the native state of the mutants, and the effect of cross-linking on the stability of a protein is not solely explained by the entropy change in denaturation. Expand
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
The results indicate that the precipitates of hen egg lysozyme are amyloid protofilament, and that the amyloids prot ofilament formation of hen Egg Lysozyme closely follows upon the destruction of the helical and tertiary structures. Expand
Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,).
The estimation of the DeltaDeltaG(HB) values of all mutant proteins after removal of hydrogen bonds, including protein-water hydrogen Bonds, indicates a favorable contribution of the intra- and intermolecular hydrogen bonds to the protein stability. Expand
A new scale for side-chain contribution to protein stability based on the empirical stability analysis of mutant proteins.
A new scale for the side-chain contribution to protein stability is proposed, derived from data on protein denaturation experiments using systematic and comprehensive mutant proteins, which has the advantage over the previously reported hydrophobicity scales of residues with the contributions of hydrogen bonds or secondary structural propensity. Expand
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.
The stability of the protein substituted at this position, which is buried in the interior of the molecule, tended to increase linearly with increasing hydrophobicity of the substituted residue, unless the volume of the substitute residue was over a certain limit. Expand
Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants.
X-ray analyses showed that the overall structures of all the mutant human lysozymes examined were identical to that of the wild-type protein, and only small structural rearrangements were observed locally around some of the mutation sites. Expand
Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus.
Analysis of the PfMAP structure in comparison with EcMAP and other mesophile proteins reveals several factors which may contribute to the hyperthermostability of PfMAP: a significantly high number of hydrogen bonds and ion-pairs between side-chains of oppositely charged residues involved in the stabilization of helices. Expand
Contribution of salt bridges near the surface of a protein to the conformational stability.
It is found that the contributions correlate with the solvent inaccessibility of the salt bridges; the salt bridge contribution was small when 100% accessible, while it was about 9 kJ/mol if 100% inaccessible, indicating how to reconcile a number of conflicting reports about role of surface salt bridges in protein stability. Expand
Contribution of water molecules in the interior of a protein to the conformational stability.
It was concluded that a water molecule in a cavity created in the interior of a protein contributes favorably to the stability of the protein. Expand