Ronald Eheman
05-05-2005, 07:31 AM
check this out !!!!
http://www.digibio.com/cgi-bin/node.pl?nd=n0
http://www.digibio.com/cgi-bin/node.pl?nd=n5
the proposed theory: "electromagnetic signals"
using various experimental protocols we are able to activate
specific cell functions with the corresponding low frequency
(<20khz) electromagnetic waves. this prompted us to hypothesize that
the molecular signal is composed of such low frequency waves and
that the ligand coresonates with the receptor pretty much as the
tuning of a radio device.
it is important to remark that these concepts do not violate any
current biological or physical basic principle. it is well-
documented that:
1) molecules emit specific frequencies;
2) a complex set of high frequency waves can produce low frequencies
according to the "beat frequency" phenomenon,
3) all biological interactions occur in water, since, on the
average, there are ten thousand molecules of water per molecule of
protein.
quantum electrodynamics calls for the existence of long range
electromagnetic fields that can be transmitted by large - hundreds
of angstroms - coherent domains present in water (adapted from e.
del giudice & e. preparata, 1994, journal of biological physics,
vol. 20, p. 105). such long range em fields would be capable of
transmitting the em message coming from molecules, thus generating a
long distance specific attraction between two molecules with
matching spectra, excluding non-resonating, unwanted random events.
the field resulting from the aggregation of the two coresonating
molecules would obviously exhibit a different frequency which would
then coresonate with the next molecule or cluster of molecules which
intervene in the next step of the biochemical reaction, and so forth
and so on... the fact that small changes in the spectrum of a
molecule (e.g. induced by a tiny structural change) would profoundly
alter its resonating characteristics, would explain how minute
changes (e.g. phosphorylation, replacement of an ion by a similar
one, switching of two peptides...) radically modify the molecular
tertiary structure and function.
http://www.digibio.com/cgi-bin/node.pl?nd=n0
http://www.digibio.com/cgi-bin/node.pl?nd=n5
the proposed theory: "electromagnetic signals"
using various experimental protocols we are able to activate
specific cell functions with the corresponding low frequency
(<20khz) electromagnetic waves. this prompted us to hypothesize that
the molecular signal is composed of such low frequency waves and
that the ligand coresonates with the receptor pretty much as the
tuning of a radio device.
it is important to remark that these concepts do not violate any
current biological or physical basic principle. it is well-
documented that:
1) molecules emit specific frequencies;
2) a complex set of high frequency waves can produce low frequencies
according to the "beat frequency" phenomenon,
3) all biological interactions occur in water, since, on the
average, there are ten thousand molecules of water per molecule of
protein.
quantum electrodynamics calls for the existence of long range
electromagnetic fields that can be transmitted by large - hundreds
of angstroms - coherent domains present in water (adapted from e.
del giudice & e. preparata, 1994, journal of biological physics,
vol. 20, p. 105). such long range em fields would be capable of
transmitting the em message coming from molecules, thus generating a
long distance specific attraction between two molecules with
matching spectra, excluding non-resonating, unwanted random events.
the field resulting from the aggregation of the two coresonating
molecules would obviously exhibit a different frequency which would
then coresonate with the next molecule or cluster of molecules which
intervene in the next step of the biochemical reaction, and so forth
and so on... the fact that small changes in the spectrum of a
molecule (e.g. induced by a tiny structural change) would profoundly
alter its resonating characteristics, would explain how minute
changes (e.g. phosphorylation, replacement of an ion by a similar
one, switching of two peptides...) radically modify the molecular
tertiary structure and function.