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Saburo Neya

Researcher at Chiba University

Publications -  188
Citations -  2965

Saburo Neya is an academic researcher from Chiba University. The author has contributed to research in topics: Heme & Myoglobin. The author has an hindex of 26, co-authored 187 publications receiving 2780 citations. Previous affiliations of Saburo Neya include Tokyo Institute of Technology & Kyoto Pharmaceutical University.

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Stoichiometries and Equilibrium Constants of Cyclodextrin-Surfactant Complexations.

TL;DR: In this article, a general and rigorous theory for equilibrium concentrations of uncomplexed species and 1 : 1, 1 : 2, 2 : 1 and 2 : 2 complexes of cyclodextrin (D) and surfactant has been developed and applied to evaluate the binding constants of these complexations from surface tension data of aqueous solutions of dodecyl maltoside (DM) with α-, β-, and γ-D, reported by Saeger and Muller-Fahrnow.
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Computational simulations of HIV-1 proteases-multi-drug resistance due to nonactive site mutation L90M

TL;DR: The difference in levels of resistance to the three inhibitors has been explained from energetic and structural viewpoints, which provides the suggestion for promising drugs keeping its efficacy even for the L90M mutant.
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Proton NMR Study of α-Cyclodextrin Inclusion of Short-Chain Surfactants

TL;DR: In this article, the binding constants and solution structures of α-cyclodextrin (α-CD) complexes with hexyltrimethylammonium (HTAB) and OTAB bromides were determined from the best correlations between the ROE intensities and the interproton distances.
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Formation of GM1 Ganglioside Clusters on the Lipid Membrane Containing Sphingomyeline and Cholesterol

TL;DR: A comparison in distribution of lipid molecules between the two kinds of membranes suggested that cholesterol had important roles to prevent the membrane from interdigitation and to stabilize other lipids for interacting with each other.
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Computational Characterization of Structural Role of the Non-active Site Mutation M36I of Human Immunodeficiency Virus Type 1 Protease

TL;DR: Results show that M36I regulates the size of the binding cavity of the protease, and the reason for the rare emergence of D30N variants in non-subtype B HIV-1 proteases was clarified from the computational analysis.