• Publications
  • Influence
Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides.
A method is described for the inclusion of the effects of hydration in empirical conformational energy computations on polypeptides. The free energy of hydration is composed of additive contributionsExpand
  • 622
  • 14
Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteins.
Understanding the role of various interactions in enhancing the thermostability of proteins is important not only for clarifying the mechanism of protein stability but also for designing stableExpand
  • 204
  • 10
Hydration and heat stability effects on protein unfolding.
  • M. Oobatake, T. Ooi
  • Chemistry, Medicine
  • Progress in biophysics and molecular biology
  • 1993
In summary, the thermal denaturation of proteins has been elucidated in terms of the chain free energy and the hydration free energy as follows. (1) Method to calculate the unfolding free energy. TheExpand
  • 156
  • 5
ProTherm: Thermodynamic Database for Proteins and Mutants
TLDR
The first release of the Thermodynamic Database for Proteins and Mutants (ProTherm) contains more than 3300 data of several thermodynamic parameters for wild type and mutant proteins. Expand
  • 137
  • 5
  • PDF
Salt‐dependent monomer–dimer equilibrium of bovine β‐lactoglobulin at pH 3
Although bovine β‐lactoglobulin assumes a monomeric native structure at pH 3 in the absence of salt, the addition of salts stabilizes the dimer. Thermodynamics of the monomer–dimer equilibriumExpand
  • 126
  • 4
An analysis of non-bonded energy of proteins.
Abstract Non-bonded energy of 16 proteins was calculated using the atomic co-ordinates obtained by X-ray crystallography. The curve of total energy against the number of atoms in proteins isExpand
  • 50
  • 4
Thermal Stability of Escherichia coli Ribonuclease HI and Its Active Site Mutants in the Presence and Absence of the Mg2+ Ion
Escherichia coli ribonuclease HI, which requires divalent cations (Mg2+ or Mn2+) for activity, was thermostabilized by 2.6-3.0 kcal/mol in the presence of the Mg2+, Mn2+, or Ca2+ ion, probablyExpand
  • 63
  • 4
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
  • 98
  • 3
Role of structural and sequence information in the prediction of protein stability changes: comparison between buried and partially buried mutations.
Predicting mutation-induced changes in protein stability is one of the greatest challenges in molecular biology. In this work, we analyzed the correlation between stability changes caused by buriedExpand
  • 137
  • 3
Characterization of the internal motions of Escherichia coli ribonuclease HI by a combination of 15N-NMR relaxation analysis and molecular dynamics simulation: examination of dynamic models.
The backbone dynamics of Escherichia coli ribonuclease HI (RNase HI) in the picosecond to nanosecond time scale were characterized by a combination of measurements of 15N-NMR relaxation (T1, T2, andExpand
  • 46
  • 3
...
1
2
3
4
5
...