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Proteins|September 1, 1996
A comparative study of dynamic structures between phage 434 Cro and repressor proteins by normal mode analysisH Wako, M Tachikawa, A OgawaJournal of Protein Chemistry|December 1, 1989
Monte Carlo simulations of a protein molecule with and without hydration energy calculated by the hydration-shell modelH WakoJournal of Protein Chemistry|October 1, 1989
Dynamic structures of globular proteins with respect to correlative movements of residues calculated in the normal mode analysisH WakoProtein Sequences & Data Analysis|April 1, 1989
Inspection of three-dimensional structures of proteins with dynamical information from the normal mode analysisH WakoBiochimica Et Biophysica Acta|February 22, 1995
Secondary structure prediction of beta-subunits of the gonadotropin-thyrotropin family from its aligned sequences using environment-dependent amino-acid substitution tables and conformational propensitiesH Wako, S IshiiPhysical Review. E, Statistical, Nonlinear, and Soft Matter Physics|August 16, 2006
Analyses of simulations of three-dimensional lattice proteins in comparison with a simplified statistical mechanical model of protein foldingH Abe, H WakoProtein Engineering|January 7, 1999
Novel method to detect a motif of local structures in different protein conformationsH Wako, T YamatoJournal of Protein Chemistry|April 1, 1991
Distance-constraint approach to higher-order structures of globular proteins with empirically determined distances between amino acid residuesH Wako, Y KubotaJournal of Molecular Biology|May 20, 1994
Use of amino acid environment-dependent substitution tables and conformational propensities in structure prediction from aligned sequences of homologous proteins. II. Secondary structuresH Wako, T L BlundellJournal of Molecular Biology|May 20, 1994
Use of amino acid environment-dependent substitution tables and conformational propensities in structure prediction from aligned sequences of homologous proteins. I. Solvent accessibility classesH Wako, T L BlundellPageof 67