Molecular gyroscopes and biological effects of weak ELF magnetic fields

Extremely-low-frequency magnetic fields are known to affect biological systems. In many cases, biological effects display `windows' in biologically effective parameters of the magnetic fields: most dramatic is the fact that relatively intense magnetic fields sometimes do not cause appreciable effect, while smaller fields of the order of 10--100 $\mu$T do. Linear resonant physical processes do not explain frequency windows in this case. Amplitude window phenomena suggest a nonlinear physical mechanism. Such a nonlinear mechanism has been proposed recently to explain those `windows'. It considers quantum-interference effects on protein-bound substrate ions. Magnetic fields cause an interference of ion quantum states and change the probability of ion-protein dissociation. This ion-interference mechanism predicts specific magnetic-field frequency and amplitude windows within which biological effects occur. It agrees with a lot of experiments. However, according to the mechanism, the lifetime $\Gamma^{-1}$ of ion quantum states within a protein cavity should be of unrealistic value, more than 0.01 s for frequency band 10--100 Hz. In this paper, a biophysical mechanism has been proposed that (i) retains the attractive features of the ion interference mechanism and (ii) uses the principles of gyroscopic motion and removes the necessity to postulate large lifetimes. The mechanism considers dynamics of the density matrix of the molecular groups, which are attached to the walls of protein cavities by two covalent bonds, i.e., molecular gyroscopes. Numerical computations have shown almost free rotations of the molecular gyros. The relaxation time due to van der Waals forces was about 0.01 s for the cavity size of 28 angstr\"{o}ms.Comment: 10 pages, 7 figure

Use of branched-chain amino acids for reducing exercise-caused skeletal muscle damage

Introduction: Skeletal muscles damage (direct and vicarious) slows down the recovery processes in patients with injuries of the musculoskeletal system. It occurs in the early postoperative period as well. An increase in the rigidity of the skeletal muscle extracellular matrix can reduce pain, tissue swelling, and accelerate the recovery of contractility.Objective: The analyses of the effect of branched-chain amino acids (BCAAs) intake on the expression of IGF1 genes, type 1, 3 and 5 collagen, which are crucial in the composition of the skeletal muscle extracellular matrix, as well as on the muscle membrane damage against the background of chronic damage to skeletal muscles.Material and methods: 12 young healthy male subjects, skiers aged 19 (18; 22) received a placebo treatment (maltodextrin, 100 mg/kg body weight/day; n = 6) or a mixture of amino acids (leucine, isoleucine, valine – 50:25:20 mg/kg body weight/day respectively; n = 6). The treatment was received daily against the background of a large amount of aerobic high-intensity training (up to 22 hours per week). Before and after the amino acids intake a biopsy of the musculus vastus lateralis was performed, and venous blood samples were taken during the experiment.Results: The intake of leucine against the background of training led not only to a pronounced increase in the level of IGF1 protein in blood by 1.5 times (which corresponds to the literature data), but also to a trend towards an increase in the expression of IGF1Ea mRNA by 1.8 times in the skeletal muscle, and a decrease in the level of markers of muscle membranes damage – creatine phosphokinase (CPK) activity and myoglobin. In addition, changes in the IGF1-dependent collagen genes expression strongly correlated with changes in IGF1Ea expression, but not with IGF1 protein in blood (pooled group, n = 12). Thus, the intake of leucine as a part of the essential amino acids can reduce damage to skeletal muscles caused by excessive physical activity, lack of physical activity, or direct trauma.Conclusion: A 10-week BCAAs intake by individuals with documented chronic muscle membrane damage caused an increase of basal levels of IGF1 in blood and a trend towards increased IGF1Ea mRNA expression in skeletal muscle, and also caused a modest reduction in damage of skeletal muscle membrane

New mechanism of solution of the kTkT-problem in magnetobiology

The effect of ultralow-frequency or static magnetic and electric fields on biological processes is of huge interest for researchers due to the resonant change of the intensity of biochemical reactions although the energy in such fields is small. A simplified model to study the effect of the weak magnetic and electrical fields on fluctuation of the random ionic currents in blood and to solve the $k_BT$ problem in magnetobiology is suggested. The analytic expression for the kinetic energy of the molecules dissolved in certain liquid media is obtained. The values of the magnetic field leading to resonant effects in capillaries are estimated. The numerical estimates showed that the resonant values of the energy of molecular in the capillaries and aorta are different: under identical conditions a molecule of the aorta gets $10^{-9}$ times less energy than the molecules in blood capillaries. So the capillaries are very sensitive to the resonant effect, with an approach to the resonant value of the magnetic field strength, the average energy of the molecule localized in the capillary is increased by several orders of magnitude as compared to its thermal energy, this value of the energy is sufficient for the deterioration of the chemical bonds.Comment: 10 pages, Accepted to the Journal Central European Journal of Physic

A human CCT5 gene mutation causing distal neuropathy impairs hexadecamer assembly in an archaeal model

Chaperonins mediate protein folding in a cavity formed by multisubunit rings. The human CCT has eight non-identical subunits and the His147Arg mutation in one subunit, CCT5, causes neuropathy. Knowledge is scarce on the impact of this and other mutations upon the chaperone’s structure and functions. To make progress, experimental models must be developed. We used an archaeal mutant homolog and demonstrated that the His147Arg mutant has impaired oligomeric assembly, ATPase activity, and defective protein homeostasis functions. These results establish for the first time that a human chaperonin gene defect can be reproduced and studied at the molecular level with an archaeal homolog. The major advantage of the system, consisting of rings with eight identical subunits, is that it amplifies the effects of a mutation as compared with the human counterpart, in which just one subunit per ring is defective. Therefore, the slight deficit of a non-lethal mutation can be detected and characterized

Optical switching of radical pair conformation enhances magnetic sensitivity

The yield of chemical reactions involving intermediate radical pairs is influenced by magnetic fields well beyond the levels expected from energy considerations. This dependence can be traced back to the microscopic dynamics of electron spins and constitutes the basis of the chemical compass. Here we propose a new experimental approach based on molecular photoswitches to achieve additional control on the chemical reaction and to allow short-time resolution of the spin dynamics. Our proposal enables experiments to test some of the standard assumptions of the radical pair model and improves the sensitivity of chemical magnetometers by two orders of magnitude

Study of the ηπo\eta\pi^o system in the mass range up to 1200 MeV

The reaction $\pi^-p \to \eta\pi^o n$ has been studied with GAMS-2000 spectrometer in the secondary 38 GeV/c $\pi^-$-beam of the IHEP U-70 accelerator. Partial wave analysis of the reaction has been performed in the $\eta\pi^o$ mass range up to 1200 MeV. The $a_0(980)$-meson is seen as a sharp peak in S-wave. The $t$-dependence of $a_0(980)$ production cross section has been studied. Dominant production of the $a_0(980)$ at a small transfer momentum $t$ confirms the hypothesis of Achasov and Shestakov about significant contribution of the $\rho_2$ exchange ($I^GJ^{PC}=1^+2^{--}$) in the mechanism of $a_0(980)$ meson production in $t$-channel of the reaction.Comment: 4 pages, 3 figures, talk given at HADRON'9

Disulfide Bridges Remain Intact while Native Insulin Converts into Amyloid Fibrils

Amyloid fibrils are β-sheet-rich protein aggregates commonly found in the organs and tissues of patients with various amyloid-associated diseases. Understanding the structural organization of amyloid fibrils can be beneficial for the search of drugs to successfully treat diseases associated with protein misfolding. The structure of insulin fibrils was characterized by deep ultraviolet resonance Raman (DUVRR) and Nuclear Magnetic Resonance (NMR) spectroscopy combined with hydrogen-deuterium exchange. The compositions of the fibril core and unordered parts were determined at single amino acid residue resolution. All three disulfide bonds of native insulin remained intact during the aggregation process, withstanding scrambling. Three out of four tyrosine residues were packed into the fibril core, and another aromatic amino acid, phenylalanine, was located in the unordered parts of insulin fibrils. In addition, using all-atom MD simulations, the disulfide bonds were confirmed to remain intact in the insulin dimer, which mimics the fibrillar form of insulin

Search for the decay KL0→3γK_L^0 \rightarrow 3\gamma

We performed a search for the decay $K_L^0 \rightarrow 3\gamma$ with the E391a detector at KEK. In the data accumulated in 2005, no event was observed in the signal region. Based on the assumption of $K_L^0 \rightarrow 3\gamma$ proceeding via parity-violation, we obtained the single event sensitivity to be $(3.23\pm0.14)\times10^{-8}$, and set an upper limit on the branching ratio to be $7.4\times10^{-8}$ at the 90% confidence level. This is a factor of 3.2 improvement compared to the previous results. The results of $K_L^0 \rightarrow 3\gamma$ proceeding via parity-conservation were also presented in this paper