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Biochemistry|May 26, 2004
Key elements for protein foldability revealed by a combinatorial approach among similarly folded but distantly related proteinsSayuri Morimoto, Atsuo TamuraPeptides|January 30, 2010
Designed low amphipathic peptides with alpha-helical propensity exhibiting antimicrobial activity via a lipid domain formation mechanismNaoki Yamamoto, Atsuo TamuraBiomacromolecules|January 18, 2014
Designing cell-aggregating peptides without cytotoxicityNaoki Yamamoto, Atsuo TamuraThe FEBS Journal|March 19, 2009
Solubility-dependent structural formation of a 25-residue, natively unfolded protein, induced by addition of a seven-residue peptide fragmentMitsugu Araki, Atsuo TamuraProteins|December 21, 2006
Transformation of an alpha-helix peptide into a beta-hairpin induced by addition of a fragment results in creation of a coexisting stateMitsugu Araki, Atsuo TamuraBiophysical Chemistry|May 13, 2025
Effects of perturbation of the hydrophobic coiled-coil core on the thermal transition process of α-helical self-assembling peptides with α-β conformational transition capabilityMinami Kurokawa, Shota Nakagawa, Atsuo TamuraThe Journal of Physical Chemistry. B|December 5, 2014
Temperature and Hydration Dependence of Low-Frequency Spectra of Lipid Bilayers Studied by Terahertz Time-Domain SpectroscopyNaoki Yamamoto, Tomoyo Andachi, Atsuo Tamura, et al.Journal of Molecular Biology|March 28, 2002
Structure of POIA1, a homologous protein to the propeptide of subtilisin: implication for protein foldability and the function as an intramolecular chaperoneHiroaki Sasakawa, Sosuke Yoshinaga, Shuichi Kojima, et al.The Journal of Physical Chemistry. B|May 10, 2016
Broadband Dielectric Spectroscopy on Lysozyme in the Sub-Gigahertz to Terahertz Frequency Regions: Effects of Hydration and Thermal ExcitationNaoki Yamamoto, Kaoru Ohta, Atsuo Tamura, et al.Physical Chemistry Chemical Physics : PCCP|August 15, 2008
Structural changes of poly-L-lysine in solution and lyophilized formOhki Kambara, Atsuo Tamura, Akira Naito, et al.Pageof 4