J. Biomedical Science and Engineering, 2008, 1, 152-156
Published Online November 2008 in SciRes. http://www.srpublishing.org/journal/jbise JBiSE
Extrinsic electromagnetic fields, low frequency
(phonon) vibrations, and control of cell function:
a non-linear resonance system
Glen A. Gordon
Electromagnetic Research and Education Foundation, PO BOX 124, Port Gamble, WA 98364. Correspondence should be addressed to Glen A. Gordon (drgor-
[e-mail]), Tel.: [phone].
Received August 21, 2008; revised September 10, 2008; accepted September 10, 2008
ABSTRACT
Chou and Chen’s report in the 1970s suggested
conformational protein adaptation (CPA) might be
influenced by low frequency phonons acting as
“a possible information system”. This report
proposes the universal force of electromagnetism
initiates the phonon system they cited as it per-
turbs paramagnetic/diamagnetic dampers within
the protein matrix to produce a quantized low
frequency phonon signal series.
(http://www.phy.ilstu.edu/~ren/phononsims/page3
.html) The signal series is iteratively processed
by the protein beta subunit, the system, to posi-
tion the alpha subunit, the outcome, a classic
non-linear resonance system resulting in con-
formational protein adaptation (CPA).
CPA “priming” enables a secondary ATP/redox
driven power system to complete cell activity. The
evolutionary appearance of these two systems
reflects their hierarchy: 1) a low energy phonon
driven information control circuit governed by
principles of physics that, along with proteins,
may have preceded planet earth, and 2), an
ATP/redox power completion circuit directed by
principles of chemistry that evolved in living
systems 1 billion or more years after earth
formed.
Keywords: Electromagnetic fields-forcer;
Paramagnetic/diamagnetic oscillators-damper;
Phonon resonance-signal series; Protein itera-
tion-system; Conformational adapta-
tion-outcome
1. INTRODUCTION
Following the “big bang” and earlier formation of para-
magnetic hydrogen, star collapse largely completed the
atomic chart with three forms of electromagnetic respon-
sive elements, i.e. paramagnetic, diamagnetic, and ferro-
magnetic; later, atmospheric damping of electromagnetic
discharges from lightning and solar sources evolved The
Schumann Resonance(SR). As life evolved on earth the
SR was the primary forcer that caused bond length oscilla-
tions in paramagnetic/diamagnetic constructs (PDCs) that
proteins strategically assembled to initiate and route the
resultant quantized signal series. In forcing this signal se-
ries that was native to the protein matrix, the SR controlled
conformational protein adaptation (CPA) in DNA, protein
enzymes, and membrane proteins. Hawking noted in A
Brief History of Time, “the universal force of electromag-
netism controls all biological response”, applicable here
just as in Pauling’s more classical derivation (Nobel lec-
ture, 1954). Diurnal fluctuations shared by living systems
and The SR constitute epochal evidence that native pho-
non vibrations are shared among proteins to control cell
function throughout the hierarchy of living systems. For
those who would assign diurnal function to light and dark
a review [48] of this atmospheric influence is suggested.
This phonon system, symbiotically shared as proteins as-
sembled, and later called a meridian, was functioning
nearly 2 billion years before the first nerve network
evolved in Cnidarians.
(http://trc.ucdavis.ed u/biosci10v /bis10v/week10/07nerv ev
olution.) “Lacking a connection to the central nervous
system” may not be a valid criticism of the meridian con-
cept.
Information Control Circuit:
The low frequency phonon control circuit is a classic
non-linear resonance system that involves iterative proc-
essing of this quantized acoustic series by beta sub-units in
enzymes, DNA, and membrane proteins, i.e. the system, to
conformationally adapt the alpha sub-unit, the outcome.
With appropriate “energy coupling” facilitated, ATP/redox
power completion dynamics shuttle ions and substrate
along metabolic pathways, but only after CPA enables that.
When investigated as a focus of life science or clinical
research, these completion dynamics should be recognized
as a separate rote activity for if activated without informed
conformational protein adaptation the result would be cha-
otic or failed cell function.
While subthreshold in themselves, appropriately
damped quantized phonon energy conducts heat and sound
through proteins as native low frequency (phonon) vibra-
tions to achieve resonance with harmonics from other
SciRes Copyright © 2008

G. A. Gordon / J. Biomedical Science and Engineering 1 (2008) 152-156 153
SciRes Copyright © 2008 JBiSE
strategically assembled paramagnetic/diamagnetic con-
structs (PDCs) within the protein thus enhancing signal
intensity several magnitudes [35]. DNA, and other pro-
teins, given their sophisticated capacity to selectively ex-
tract harmonics, use these signals in combination with
other “noise”, i.e. stochastic resonance, to enhance protein
function [6, 18, 44]. This selective matching indicates a
sophisticated routing capacity in proteins [33, 34] which is
proposed here to be a co-activity of PDCs. An area of in-
vestigative interest in this regard may be the mag-
neto-hydrodynamic effects described by Alfven (Nobel
lecture, 1970) and a recent report on Hall effects [50] in
phonons
This initiating/routing phonon information system
promises market disruptive technologies that could dra-
matically enhance homeostasis as a system undergoes
ischemia-reperfusion injury or other insult [12]. Extant
literature [24, 31, 38] suggests significant potential for
designed electromagnetic pulsed therapies (DEPTH), the
technology to replace classes of drugs and numerous sur-
geries within the decade.
2. HISTORY
The Flexner Report in 1910 declared the universal force of
electromagnetism “irregular science” and it was purged
from medical curricula in the United States forty-five
years after Maxwell defined it; a similar effort in Europe
was unsuccessful. 1900 and “The New Era of Science”
saw electromagnetism eventually characterized as “con-
trolling all chemical reactions, including life itself” [25].
Considering this universal force and its influence on
chemical reactions, it is inexplicable that clinical, biologi-
cal, and basic science interest in electromagnetism, PDCs,
and their relation to cell function languished until MRI
stimulated interest in the late 20th century.
3. NORMAL MODE (ELEMENTARY) PHO-
NON VIBRATIONS
Kuo-Chen Chou developed an iconic archive on the im-
portance of low frequency phonon vibrational activity in
proteins following his original insight [17]. He considered
low frequency vibrations (phonons) in proteins including
DNA implicit to their biological function [13, 14, 15, 16].
In citing the “overwhelming production of phonons by
native low frequency vibrations”, and, “the importance of
low frequency vibrations in biologic function from the
viewpoint of both thermodynamic and molecular dynam-
ics”, he alluded to the conformational adaptation of pro-
teins and control of cell function in response to these na-
tive low frequency vibrations as, “an intriguing concept”.
W. Ross Adey accumulated an archive [1, 2, 3] on
non-linear EMF cellular effects and intrinsic communica-
tion systems between cells that he considered, “a general
biologic property”. Adey’s early soliton concept [36] was
later abandoned by his co-author [37].
All constituent elements and amino acids function as
PDC dampers within a protein lattice where, if the EM
field is appropriate, an elementary or “native” mode pho-
non vibration results that is compatible with individual
protein design and length. Given this as the means for
generating phonons, Kriegl et als [33] report additionally
suggests a routing effect exists in biological systems,
which prompts the question, “Does electromagnetism in-
fluence PDCs to generate phonons and direct their routing
as well?” Sophisticated phonon initiation and routing di-
rects conformational protein adaptation to prime redox
reactions [52], calcium channel activity, and bioenergetics
[17]; up-regulating DNA [12, 49] and enhancing enzyme
activity [55] as iterative outcomes are proposed as logical
conclusions in other reports,
Curie’s magnetic moment (M) of a paramagnetic spe-
cies, which represents the sum of EMF directed dipole
alignment (B), and Brownian vibrational activity (T), is
the energy transduced into the protein lattice with sophis-
ticated forward and reverse options [34, 27] to remote sites
[6,18, 29,44]. When an EM field is damped to create a
native (elementary) vibrational activity it assures homeo-
static CPA as the system experiences challenge.
Johnson et al. [30] noted “unambiguous” evidence for
PDC presence in Fe/enzyme models, and Ubbink et al. [52]
reported that PDC forces directed conformational protein
changes that resulted in apposition of distant protein redox
sites and ensuing reaction, redox chemistry controlled by
principles of physics.
“Stochastic resonance” is the ability of proteins to guide
appropriate harmonics extracted from “noise”, to sum with
sub-threshold phonon harmonics, another highly evolved
adaptive response to enhance sub-threshold native or ele-
mentary signal series. It is unimaginable to consider that
proteins would evolve a means to generate phonons with-
out a means to route them.
If time is an essential component in non-linear events
[25], it should be noted that others report such distant site
activations are tightly tied to protein conformational
changes [51, 52], and sequential ligand relaxation times
[51]. Additionally, others [33, 42] corroborate Anfinsen’s
1972 Nobel Prize findings that protein function is highly
dependent on pH to speed or slow the process. For decades
“classicist” argument has refuted non-linearity in cell sig-
naling, however the iteration of quantized phonon signal
series is a non-linear process
http://www.p hy.ilstu.edu /~ren/phononsims/ page3.html). In
combination with the other inter-dependent variables it
would appear a classic linear solution is an antiquated
proposal.
4. ELECTRO-POLLUTION;
NON-ELEMENTARY VIBRATIONS
Based upon Curie’s Law, (M=k B/T), if the imposed EM
field (B) saturates PDC dipole alignment sufficiently,
which need not be complete, their “damper” ability is
compromised. In such an event it would seem possible to
introduce extrinsic, “non-elementary modes” to cause
structural or functional failure of “the system” if incom-
patible with the protein lattice’s ability to absorb them.
Outcomes possible when a harmonic forcer drives a sys-

154 G. A. Gordon / J. Biomedical Science and Engineering 1 (2008) 12-156
SciRes Copyright © 2008 JBiSE
tem are: 1. the system changes design, e.g. a swing angle,
2. energy output must equal energy input, 3. the system
fails. As noted in Fundamentals In Physics, [26], “care
must be taken not to subject a system to a strong external
driving force . . . or the resulting oscillations may rupture
it”. Item 2 suggests that when heat energy in exceeds en-
ergy out the protein may be denatured resulting in a func-
tional failure. The non-elementary vibrations associated
with an EM force capable of saturating dipole activity and
nullifying damping by PDCs are proposed as such oscilla-
tions. DNA due to its size, design, and quantity of elec-
tromagnetic responsive constructs may be quintessentially
vulnerable to non-elementary resonant energy.
Elementary vs non-elementary dynamics must be con-
sidered when “lumping” therapeutic and “elec-
tro-pollution” field effects since one is designed to be na-
tive to the protein and the others non-elementary energy
that must follow outcomes two or three. Switching large
field strengths create field gradients that strongly argue
against a “more is better” approach in DEPTH applica-
tions, e.g. rTMS and treatment of depression.
The upside of non-elementary resonant vibration sug-
gests its use to destroy infectious pathogens. HIV and
other pathogens undergo vulnerable dynamic adaptations,
e.g. g41 fusion protein, that promise compromised func-
tion or structure with appropriate vibrational exposure
Successful eradication of Plasmodium falciparum in
Ghana after a single DEPTH treatment has been reported
[22]; that report cites a different vibrational mechanism
than is suggested here.
Trial and error will be necessary to find non-elementary
vibrational modes necessary to degrade the function or
structure of vulnerable proteins. Anecdotal observations
over 25 yrs on treating infectious conditions with DEPTH,
e.g. fistuli, otitis, lymphangitis, suggests the originating
EM field can be within therapeutic limits with outcomes
that indicate a startlingly rapid functional or structural
compromise of agent virulence, if not viability. Satisfied
with the rapid dehiscence of pain and inflammation, one
overlooked the obvious implication in permanently im-
proved outcomes that required no additional treatment.
Toxic metals and chemical toxins may substitute very
different energy into PDC bonds, which then oscillate at
very different output modes than the original construct to
create a “non-elementary” response to an otherwise nor-
mal EM force, perhaps the long-term lethal threat in such
bond substitutions.
5. ELECTROGENOMICS
The use of designed EM pulses to up-regulate DNA re-
ceived substantial support when the Columbia University
group headed by Blank and Goodman reported that
site-specific electromagnetic responsive elements (EMREs)
regulate DNA synthesis [11, 40]. In spite of their observa-
tion these authors propose other than paramag-
netic/diamagnetic dynamics, signal series, and conforma-
tional adaptation of DNA to activate gene loci. It could be
proposed that electron transit across weak hydrogen bonds
between base amino acid pairs doesn’t occur “de novo”,
which suggests such enthalpy is an iterative, conforma-
tional adaptive activity. This same group reported that
up-regulation was increased when transduced via multiple,
similar EMRE constructs vs. just one or two [40], which
strongly suggests an EMF/PDC/phonon iteration effect as
the first order mechanism. [6, 18, 44]
6. CALCIUM AND Ca++ CHANNEL
ACTIVITY
Eichwald and Walleczek [21] reported the biologi-
cal-functional status of treated tissue can result in EMF
stimulation, inhibition, or no effect, which they attributed
to “activation of specific EMF sensitive enzyme systems
that modulate calcium entry.” Calcium is an alkaline earth
metal, diamagnetic, and considered “very reactive” [56]; it
and water are both diamagnetic and highly mobile in EM
fields, which along cell membranes with their myriad
PDCs can only be imagined. Without noting its diamag-
netic nature, calcium flux in response to EM fields was
reported [39], and Dihel et al. [29] demonstrated such ob-
servations were related to Ca channel activity. Davies and
Norris [19] demonstrated that Ca++ dependent motility in
marine diatoms, was substantially enhanced by EMFs.
Using pheochromocytoma cells, Ikehara et al.[28] demon-
strated EMFs inhibit increases in cytosolic [Ca++] by lim-
iting release from intracellular stores, which was rapid (15
min) and lasted for two hours in the face of unchanged
ATP levels over that period. Gibbs et al demonstrated cys-
teine rich secretory protein domains regulate ion channel
activity, “and provide compelling evidence for a role in
[Ca++] regulation…” Cysteine is proposed a classic PDC.
Vendel et al [54] reported, “Ca++ channel beta sub-units
regulate trafficking and gating of voltage dependent Ca++
channel alpha subunits”, indicating beta subunits are the
protein intelligence that computationally processes acous-
tic signal series. Using signal series to position voltage
gated alpha subunits into appropriate position to achieve
homeostasis is the precisely computed outcome of this
“low voltage” information control circuit; given this direc-
tion, the parallel ATP driven energy system fulfills its
“power circuit” role by appropriately moving substrate and
solute to complete the homeostatic effort.
CPA (folding) has been demonstrated as a direct PDC
effect [52], and Rosen’s [47] reference to Ca++ channel
deformation from “anisotropic diamagnetic” phospolipids
in the cell membrane might be expanded to incorporate
many other PDCs [7], not to mention transitional metals.
Vendel [53] further notes, “these domains that regulate cell
surface expression and movement of Ca++ voltage gated
alpha sub-units involve five domains related to, “a large
family of membrane-associated guanylate kinase proteins”,
conformational adaptation suggested to be a (phonon) sig-
nal series driven outcome. Mustafi et al. [43] report essen-
tially similar findings in terms of multiple domains as part
of “paramagnetic interactions with diamagnetic lantha-
nides, which substitute for Ca++”.
PDCs are major contributors to conformational protein

G. A. Gordon / J. Biomedical Science and Engineering 1 (2008) 152-156 155
SciRes Copyright © 2008 JBiSE
control of Ca++ channel activity, very probably Ca++
routing through the channel, and cytosolic [Ca++] release
[28]. Lastly, Baureus Koch et al. [8] studied weak EMF
effects on the cell membrane and found, “suitable combi-
nations of time varying magnetic fields directly interact
with Ca++ channel proteins in the cell membrane”.
7. CONCLUSION
Adey noted [3], “Today we stand at a new, far more sig-
nificant frontier, and while it may be more difficult to un-
derstand, it is at the atomic level rather than the molecular
that physical rather than chemical processes shape the
flow of signals essential to living matter . . . one of the
great revolutions in the history of biology”. Adey was an
MD who spent much of his career seeking the connection
between cell function and the universal force of electro-
magnetism. This author proposes that PDC response to
electromagnetic forcers, which has been overlooked for a
century, keys the sophisticated information network pro-
teins rely upon for conformational adaptive response [1, 2,
9, 41, 45, 46, 52]. Almost as an afterthought, redox reac-
tions and ATP complete cell response.
It is apropos that we modify EB Wilson’s 1950s quote,
[4], “the key to every biologic problem must finally be
sought in the cell” to that of a 2008 version, “must finally
be sought in the physics of phonons, native low frequency
vibrations that drive conformational protein adaptation ”,
the cell will follow. Phonon physics and conformational
protein adaptation are central to the paradigm beyond mo-
lecular physiology. Recent articles [6, 18] report DNA’s
use of noise to up-regulate gene synthesis and the sophis-
ticated capacity of proteins to extract specific harmonics
from overtones to enhance sub-threshold acoustic infor-
mation. Electromagnetism both initiates and routes these
vital phonon signals to control biological response; a so-
phisticated information system would have it no other
way.
This understanding suggests overlooked avenues to
control cell function, DNA up-regulation, and enzyme
activity in response to ischemia-reperfion injury and other
threats that will be better served by technologies as op-
posed to current drug regimens and numerous surgeries.
Proteins initiated this low energy conformational adap-
tive system upon first evolving, two or more billion years
before the appearance of a nerve network, and still further
removed from a central nervous system. A step toward
returning to Rachel Carson’s, “natural balance of things”
and the human condition would be to enhance iterative
protein activity rather than “blocking” or “inhibiting” it.
REFERENCES
[1] W.R. Adey. (1988) The cellular microenvironment and signaling
through cell membranes. Progress in Clinical and Biological Re-
search 257, 81-106.
[2] W.R. Adey. (1988) Cell Membranes: The electromagnetic environ-
ment and cancer promotion. Neurochemistry Research 7, 671-677.
[3] W.R. Adey. (1993) Biologic Effects of Electromagnetic Fields.
Journal of Cellullar Biochemistry 4, 410-416.
[4] B. Alberts, D. Bray, J. Lewis, M. Raff, K. Roberts, J.D. Watson.
(1989) Molecular Biology of The Cell, 2nd Ed. New York:Garland
Publishing, preface.
[5] Angaridis P, Cotton FA, Murillo CA, Villagran D, Wang X. (2004).
Paramagnetic precursors for supramolecular assemblies: selective
syntheses, crystal structures, and electrochemical and magnetic
properties of Ru2(O2CMe)4-n(formamidinate)nCl complexes, n =
1-4. Inorganic Chemistry. Dec 26, 8290-8300.
[6] D.W. Austin, M.S. Allen, J.M. McCollum, R.D. Dar, J.R. Wilgus,
G.S. Sayler, N.F. Samatova, C.D. Cox, M.L. Simpson. (2006) Gene
network shaping of inherent noise spectra. Nature 7076, 608-611.
[7] S. Balakrishnan, N.J. Zondlo. (2006) Design of a protein
kinase-inducible domain. Journal of the American Chemical Society
17, 5590-5591.
[8] C.L. Baureus Koch, M. Sommarin, B.R. Persson, L.G. Salford, J.L.
Eberhardt. (2003) Interaction between weak low frequency magnetic
fields and cell membranes. Bioelectromagnetics 6, 395-402.
[9] R.O. Becker,. Exploring new horizons in electromedicine. Journal
Alternative and Complementary Medicine 1, 17-18.
[10] I. Bertini, A. Donaire, B. Jimenez, C. Luchinat, G. Parigi, M. Piccioli,
L. Poggi. (2001) Paramagnetism-based versus classical constraints:
an analysis of the solution structure of Ca Ln calbindin D9k. Journal
of Biomolecular NMR 2, 85-98.
[11] M. Blank, R. Goodman. (2004) Initial interactions in electromag-
netic field-induced interactions. Journal of Cellular Physiology 3,
359-363.
[12] S. Carmody, X.L. Wu, H. Lin, M. Blank, R. Goodman (2000) Cyto-
protection by electromagnetic field-induced hsp70: a model for
clinical appl;ication. J Cellular Biochem, 79: 453-459.
[13] K.C. Chou. (1984) Low-frequency vibration of DNA molecules.
Biochemical Journal 221, 27-31.
[14] K.C. Chou. (1985) Low-frequency motions in protein molecules:
beta-sheet and beta-barrel. Biophysical Journal 48, 289-297.
[15] K.C. Chou. (1988) Review: Low-frequency collective motion in
biomacromolecules and its biological functions. Biophysical Chem-
istry 30, 3-48.
[16] K.C. Chou. (1989) Low-frequency resonance and cooperativity of
hemoglobin. Trends in Biochemical Sciences 14, 212.
[17] K.C. Chou, and N.Y. Chen. (1977) The biological functions of
low-frequency phonons. Scientia Sinica 20, 447-457.
[18] C.D. Cox, J.M. McCollum, D.W. Austin, M.S. Allen, R.D. Dar, M.L.
Simpson. (2006) Frequency domain analysis of noise in simple gene
circuits. Chaos 16, 26102.
[19] M.S. Davies, W.T. Norris. (2004). Vibration as a possible explana-
tion for putative electromagnetic field effects: a case study on ma-
rine diatoms. International Journal of Radiation Biology10, 709-718.
[20] L.E. Dihel, J. Smith-Sonneborn, C.R. Middaugh. (1985) Effects of
an extremely low frequency electromagnetic field on the cell divi-
sion rate and plasma membrane of Paramecium tetraurelia. Bioelec-
tromagnetics1, 61-71.
[21] C. Eichwald, J. Walleczek. (1996) Activation-dependent and bi-
phasic electromagnetic field effects: model based on cooperative
enzyme kinetics in cellular signaling. Bioelectromagnetics 6,
427-435.
[22] J.E. Feagin, M.A. Wurschler, R. Ceon, H.C. Lai. (1999) Magnetic
Fields and Malaria, “Biologic Effects of Light: Proceedings of the
Biologic Effects of Light Symposium”. Holick, M.F. and Jung E.G.
(eds). Kluwer Academic Publishers, Higham MA, 343-349.
[23] G.M. Gibbs, M.J. Scanlon, J. Swarbrick, S. Curtis, E. Gallant, A.F.
Dulhunty, M.K. O'Bryan. (2006) The cysteine-rich secretory protein
domain of Tpx-1 is related to ion channel toxins and regulates ry-
anodine receptor Ca2+ signaling. J Biological Chemistry 7,
4156-4163.
[24] G.A. Gordon. (2007) Designed Electromagnetic Pulsed Therapy:
Clinical Uses. J Cellular Physiology, 579-582.
[25] S. Hawking. (1988) A Brief History of Time. New York: Bantam
Books. p. 61.
[26] D. Halliday, R. Resnick, J. Walker. (1993) Fundamentals of Physics,
4th Ed. New York City: John Wiley & Sons Inc., 399-400.
[27] A.R. Holzwarth, M.G. Muller. (1996). Energetics and kinetics of
radical pairs in reaction centers from Phodobacter sphaeroides. A
femtosecond transient study. Bioechemistry 36, 11820-11831.
[28] T. Ikehara, H. Yamaguchi, K. Hosokawa, H. Houchi, K.H. Park, K.

156 G. A. Gordon / J. Biomedical Science and Engineering 1 (2008) 12-156
SciRes Copyright © 2008 JBiSE
Minakuchi, H. Kashimoto, M. Kitamura, Y. Kinouchi, K. Yoshizaki,
H. Miyamoto. (2005) Effects of a time-varying strong magnetic field
on transient increase in Ca2+ release induced by cytosolic Ca2+ in
cultured pheochromocytoma cells. Biochemica Biophysica Acta 1-2,
8-16.
[29] J. Iwahara, G.M. Clore. (2006) Detecting transient intermediates in
macromolecular binding by NMR. Nature 7088, 1227-1230.
[30] M.K. Johnson, J.E. Morningstar, M. Oliver, F.E. Frerman. (1987)
Electron paramagnetic resonance and magnetic circular dichroism
studies of electron-transfer flavoprotein-ubiquinone oxireductase
from pig liver. FEBS Letters 1, 129-133.
[31] M.T. Johnson, L.R. Waite, G. Nindl. (2004) Non-invasive treatment
of inflammation using EM fields: current and emerging therapeutic
potential. Biomedical Sciences Instrumentation 40, 469-474.
[32] G.J. Kornhaber, D. Snyder, H.N. Moseley, G.T. Montelione. (2006)
Identification of zinc-ligated cysteine residues based on 13Calpha
and 13Cbeta chemical shift data. J Biomolecular NMR 4, 259-269.
[33] J.M. Kriegl, A.J. Bhattacharyya, K. Nienhaus, P. Deng, O. Minkow,
G.U. Nienhaus. (2002) Ligand binding and protein dynamics in
neuroglobin. Proceedings of the National Academy of Sciences,
USA 12, 7992-7997.
[34] J.M. Kriegl, G.U. Niehaus. (2004) Structural, dynamic, and energetic
aspects of long-range electron transfer in photosynthetic reaction
centers. Proceedings of The National Academy of Sciences, USA 1,
12312-12318.
[35] I.L. Kruglikov, H. Dertinger.(1994) Stochastic resonance as a possi-
ble mechanism of amplification of weak electric signals in living
cells. Bioelectromagnetics 6, 539-547.
[36] A.F. Lawrence, W.R. Adey. (1982). Nonlinear wave mechanisms in
interactions between excitable tissue and electromagnetic fields.
Neurological Research 4, 115-153.
[37] A.F. Lawrence et al. (1987) The Nature of Phonons and Soliton
Waves in Alpha Helical Proteins. Journal of Biophysics 51-5,
785-93.
[38] A. Liboff. (2004) Toward an electromagnetic paradigm for biology
and medicine, Journal Alternative and Complementary Medicine 1,
41-47.
[39] R.J. Lieb, W. Regelson, B. West, R.L. Jordan, D.P. DePaola. (1980)
Effect of pulsed high frequency electromagnetic radiation on em-
bryonic mouse tissue palate in vitro. Journal of Dental Research 10,
1649-1652.
[40] H. Lin, M. Blank, K. Rossol-Haseroth, R. Goodman. (2001) Regu-
lating genes with electromagnetic response elements. Journal of
Cellular Biochemistry 1, 143-148.
[41] B.R. McLeod, A.R. Liboff, S.D. Smith. (1992) Electromagnetic
gating in ion channels. Journal of Theoretical Biology 1, 15-31.
[42] O.B. Morozova, S.E. Korchak, R.Z. Sagdeev, A.V. Yurkovskaya.
(2005) Time-resolved chemically induced dynamic nuclear polariza-
tion studies of structure and reactivity of methionine radical cations
in aqueous solution as a function of pH. Journal of Physical Chem-
istry A 45, 10459-10466.
[43] S.M. Mustafi, S. Mukherjee, K.V. Chary, C. Del Bianco, C. Luchinat.
(2004) Energetics and mechanism of Ca2+ displacement by lantha-
nides in a calcium binding protein. Biochemistry 29, 9320-9331.
[44] J.M. Pedraza, A. van Oudenaarden. (2005) Noise propagation in
gene networks. Science 5717, 1965-1969.
[45] B. Rabenstein, G.M. Ullmann, E.W. Knapp. (2000) Electron transfer
between the quinones in the photosynthetic reaction center and its
coupling to conformational changes. Biochemistry 34, 10487-10496.
[46] V. Ramikrishnan, D. Henderson, D.D. Busath. (2004) Applied field
nonequilibrium molecular dynamics simulations of ion exit from a
beta-barrel model of the L-type calcium channel. Biochimica et
Biophysica Acta 1, 1-8.
[47] A.D. Rosen. (2003). Mechanism of action of moderate-intensity
static magnetic fields on biological systems. Cell Biochemistry and
Biophysics 2, 163-174
[48] A. Schenle, V. Starkand. (1998) J Scientific Exploration 12,
455-468.
[49] H.M. Sobell, C.C. Tsai, S.C. Jain, T.D. Sakore. (1978) Conforma-
tional flexibility in DNA structure and its implication in under-
standing the organization of DNA in chromatin. Philos. Trans. R.
Lond. B. Biol. Sci. 11, 295-298.
[50] C. Strohm, G..L. Rikken, P. Wyder. (2005) Phenomenologic Evi-
dence for the Phonon Hall Effect. Phys Rev Lett 95, 155901, 2005.
[51] J. Tandori, P. Sebban, H. Michel, L. Baciou. (1999) In Rhodobacter
sphaeroides reaction centers, mutation of proline L209 to aromatic
residues in the vicinity of a water channel alters the dynamic cou-
pling between electron and proton transfer processes. Biochemistry
40, 13179-13187.
[52] M. Ubbink, M. Ejdeback, B.G. Karlsson, D.S. Bendall. (1998) The
structure of the complex of plastocyanin and cytochrome f, deter-
mined by paramagnetic NMR and restrained rigid-body molecular
dynamics. Structure 3, 323-335.
[53] A.C. Vendel, C.D. Rithner, B.A. Lyons, W.A. Horne. (2006) Solu-
tion structure of the N-terminal A domain of the human volt-
age-gated Ca2+channel beta4a subunit. Protein Science 2, 378-383.
[54] A.C. Vendel, M.D. Terry, A.R. Striegel, N.M. Iverson, V. Leuranguer,
C.D. Rithner.
a) Voltage-gated Ca2+ channel beta4 subunit creates a uniquely
folded
b) N-terminal protein binding domain with cell-specific expres-
sion in the
c) cerebellar cortex. Journal of Neuroscience10, 2635-2644.
[55] M. Wang, R.T. Borchardt, R.L. Schowen, K. Kuczera. (2005) Do-
main motion and the open-to-closed conformational transition of an
enzyme: a normal mode analysis . . . Biochemistry 17, 7228-7239.
[56] S. Zumdahl. (1992) Chemical Principles. Lexington MA: DC
Heath and Co. p 980.