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1.
Med Sci Monit ; 13(1): SR1-8, 2007 Jan.
Article in English | MEDLINE | ID: mdl-17179919

ABSTRACT

According to the western medical establishment, homeopathy is both "unscientific" and "implausible". A short overview of its history and the methods it uses, however, easily reveals that homeopathy is a true science, fully grounded on the scientific method and on principles, such as, among others, the Arndt-Schultz law, hormesis, and epitaxy, whose plausibility has been clearly and definitely demonstrated in a number of scientific publications and reports. Through a review of the scientific literature, an explanation of the basic principles of homeopathy is proposed based on arguments and evidence of mainstream science to demonstrate that, in spite of the claims of conventional medicine, homeopathy is both scientific and plausible and that there is no reasonable justification for its rejection by the western medical establishment. Hopefully, this hurdle will be overcome by opening academic institutions to homeopathy to enlarge the horizons of medical practice, recover the value of the human relationship with the patient, and through all this, offer the sick a real alternative and the concrete perspective of an improved quality of life.


Subject(s)
Homeopathy , Water/chemistry , Dose-Response Relationship, Drug , Humans , Mind-Body Relations, Metaphysical , Placebo Effect , Quality of Life , Water/metabolism
2.
Homeopathy ; 93(4): 199-202, 2004 Oct.
Article in English | MEDLINE | ID: mdl-15532699

ABSTRACT

Proteins, with the large variety of chemical groups they present at their molecular surface, are a class of molecules which can be very informative on most of the possible solute-solvent interactions. Hen egg white lysozyme has been used as a probe to investigate the complex solvent dynamics occurring at the protein surface, by analysing the results obtained from Nuclear Magnetic Resonance, X-ray diffractometry and Molecular Dynamics simulations. A consistent overall picture for the dynamics of water molecules close to the protein is obtained, suggesting that a rapid exchange occurs, in a picosecond timescale, among all the possible hydration surface sites both in solution and the solid state, excluding the possibility that solvent molecules can form liquid-crystal-like supramolecular adducts, which have been proposed as a molecular basis of 'memory of water'.


Subject(s)
Egg Proteins/metabolism , Muramidase/metabolism , Protein Conformation , Water/metabolism , Animals , Chickens , Computer Simulation , Crystallography, X-Ray , Models, Chemical , Models, Molecular , Solvents
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