Theory of bio-energy transport in protein molecules and its experimental evidences as well as applications ( I )

A new theory of bio-energy transport along protein molecules, where energy is released by the hydrolysis of adenosine triphosphate (ATP), has recently been proposed for some physical and biological reasons. In this theory, Davydov’s Hamiltonian and wave function of the systems are simultaneously improved and extended. A new interaction has been added into the original Hamiltonian. The original wave function of the excitation state of single particles has been replaced by a new wave function of the two-quanta quasi-coherent state. In such a case, bio-energy is carried and transported by the new soliton along protein molecular chains. The soliton is formed through the self-trapping of two excitons interacting with amino acid residues. The exciton is generated by the vibration of amide-I (C=O stretching) arising from the energy of the hydrolysis of ATP. The properties of the soliton are extensively studied by analytical methods and its lifetime for a wide range of parameter values relevant to protein molecules is calculated using the nonlinear quantum perturbation theory. The lifetime of the new soliton at the biological temperature of 300 K is large enough and belongs to the order of 10^-10 s or τ/τ₀ ≥ 700. The different properties of the new soliton are further studied. The results show that the new soliton in the new model is a better carrier of bio-energy transport and it can play an important role in biological processes. This model is a candidate of the bio-energy transport mechanism in protein molecules.     

The lifetime of the soliton in the improved Davydov model at the biological temperature 300 K for protein molecules

We study the effects of quantum fluctuations and thermal perturbations on the lifetime of the soliton in the improved Davydov model proposed by us with two-quanta and with an added interaction. By using quantum perturbation theory, we compute the soliton lifetime for a wide ranges of parameter values relevant for protein molecules. The lifetime of the new soliton at the biological temperature 300 K is of the order of 10^-10 second or τ/τ≥ 500 for parameters appropriate to α-helical protein molecules. This shows clearly that the new soliton in the improved model is a viable mechanism for the bio-energy transport in the α-helix region of proteins. Received 7 January 1999 and Received in final form 16 August 2000     

The theory of bio-energy transport in the protein molecules and its properties

The bio-energy transport is a basic problem in life science and related to many biological processes. Therefore to establish the mechanism of bio-energy transport and its theory have an important significance. Based on different properties of structure of α-helical protein molecules some theories of bio-energy transport along the molecular chains have been proposed and established, where the energy is released by hydrolysis of adenosine triphosphate (ATP). A brief survey of past researches on different models and theories of bio-energy, including Davydov's, Takeno's, Yomosa's, Brown et al.'s, Schweitzer's, Cruzeiro-Hansson's, Forner's and Pang's models were first stated in this paper. Subsequently we studied and reviewed mainly and systematically the properties, thermal stability and lifetimes of the carriers (solitons) transporting the bio-energy at physiological temperature 300 K in Pang's and Davydov's theories. From these investigations we know that the carrier (soliton) of bio-energy transport in the α-helical protein molecules in Pang's model has a higher binding energy, higher thermal stability and larger lifetime at 300 K relative to those of Davydov's model, in which the lifetime of the new soliton at 300 K is enough large and belongs to the order of 10(-10) s or τ/τ(0)≥700. Thus we can conclude that the soliton in Pang's model is exactly the carrier of the bio-energy transport, Pang's theory is appropriate to α-helical protein molecules.     

INVESTIGATION OF PROPERTIES OF INFRARED ABSORPTION OF α-HELIX PROTEIN MOLECULES

The mechanism and properties of infrared absorption of α-helix protein molecules are studied by a theory of bio-energy transport established on the basis of molecular structure. From the vibrational energy-spectra of molecules obtained from this theory we know that the infrared lights with wavelengths of 2 μm −7 μm can be absorbed by α-helix protein molecules. This is basically consistent with experimental data of infrared absorption of collagen and hemoglobin and bivine serum albumen (BSA) proteins with α-helix structure. From these results we account further for the mechanism and properties of biological effect of infrared lights absorbed by the living systems, i.e., the energy of infrared lights is directly absorbed by the amide-Is in amino acid residues in the protein molecules, which results in vibration of amide-1 and change of conformation of proteins and transport of bio-energy from one place to other along the protein molecular chains in human beings and animals. This is a kind of non-thermally biological effect.     

Changes of properties of the soliton with temperature under influences of structure disorder in the α-helix protein molecules with three channels

The changes of property of solitons in α-helix protein molecules with three channels under influences of fluctuations of structure parameters and thermal perturbation of medium are extensively investigated using dynamic equations in the improved theory, numerical simulation and Runge-Kutta method. In this investigation the peculiarities of the solitons are given first in the motions of short-time and long-time and its collision features at T = 0 K and biological temperature T = 300 K. This study shows that the solutions of dynamic equations are solitons, which are very stable at T = 0 and 300 K, although its amplitudes and velocity are somewhat decreased relative to that at T = 0 K, the soliton can transport over 1000 amino acid residues, its lifetime is, at least, 120 ps. Subsequently, studies are made of the changes of properties of the soliton with variations of temperature of the medium and fluctuations of structure parameters including mass sequence of amino acid residues and the coupling constant, force constant, dipole–dipole interaction, chain–chain interaction and ground state energy in the α-helix proteins. The investigations indicate that the soliton has high thermal stability and can transport along the molecular chains retaining amplitude, energy and velocity, although the fluctuations of the structure parameters and temperature of the medium increase continually. However, the solitons disperse in larger fluctuations at T = 300 K and higher temperatures than 315 K. Thus it is determined that the critical temperature of the soliton is 315 K. Finally reasons are given for the generation of high thermal stability of the soliton and the correctness of the improved model is demonstrated. It is concluded that the soliton in the improved model is very robust against structure disorder and thermal perturbation of the α-helix protein molecules at 300 K, and is a possible carrier of bio-energy transport, and the improved model is maybe a candidate for the mechanism of this transport.     

Stabilization of the Soliton Transported Bio-energy in Protein Molecules in the Improved Model

We study the stabilization of the soliton transported bio-energy by the dynamic equations in the improved Davydov theory from four aspects containing the feature of free motion and states of the soliton at the long-time motion and at biological temperature 300 K and behaviors of collision of the solitons by Runge-Kutta method and physical parameter values appropriate to the $\alpha$-helix protein molecules. We prove that the new solitons can move without dispersion at a constant speed retaining its shape and energy in free and long-time motions and can go through each other without scattering. If considering further influence of the temperature effect of heat bath on the soliton, it is still thermally stable at biological temperature 300 K and in a time as long as 300 ps and amino acid spacings as large as 400, which shows that the lifetime of the new soliton is at least 300 ps, which is consistent with analytic result obtained by quantum perturbation theory. These results exhibit that the new soliton is a possible carrier of bio-energy transport and the improved model is possibly a candidate for the mechanism of this transport.     

Influences of Quantum and Disorder Effects on Solitons Excited in Protein Molecules in Improved Model

Utilizing the improved model with quasi-coherent two-quantum state and new Hamiltonian containing an additional interaction term [Phys. Rev. E62 (2000) 6989 and Euro. Phys. J. B19 (2001) 297] we study numerically the influences of the quantum and disorder effects including distortion of the sequences of masses of amino acid molecules and fluctuations of force constant of molecular chains, and of exciton-phonon coupled constants and of the dipole-dipole interaction constant and of the ground state energy on the properties of the solitons transported the bio-energy in the protein molecules by Runge-Kutta method. The results obtained show that the new soliton is robust against these structure disorders, especially for stronger disorders in the sequence of masses spring constants and coupling constants, except for quite larger fluctuations of the ground state energy and dipole-dipole interaction constant. This means that the new soliton in the improved model is very stable in normal cases and is possibly a carrier of bio-energy transport in the protein molecules.     

Bio-energy in s-Helix Protein Molecules with Three Properties of Soliton-Transported Channels

We study numerically the propagating properties of soliton-transported bio-energy excited in the a-helix protein molecules with three channels in the cases of the short-time and long-time motions and its features of collision at temperature T = 0 and biological temperature T = 300 K by the dynamic equations in the improved Davydov theory and fourth-order Runge-Kutta method, respectively. From these simulation experiments we see that the new solitons in the improved model can move without dispersion at a constant speed retaining its shape and energy in the cases of motion of both short-time or T = 0 and long time or T = 300 K and can go through each other without scattering in their collisions. In these cases its lifetime is, at least, 120 ps at 300 K, in which the soliton can travel over about 700 amino acid residues. This result is consistent with analytic result obtained by quantum perturbed theory in this model. In the meanwhile, the influences of structure disorder of a-helix protein molecules, including the inhomogeneous distribution of amino acids with different masses and fluctuations of spring constant, dipole-dipole interaction, exciton-phonon coupling constant and diagonal disorder, on the solitons are also studied by the fourth-order Runge-Kutta method. The results show that the soliton still is very robust against the structure disorders and thermal perturbation of proteins at biological temperature 300 K. Therefore we can conclude that the new soliton in the a-helix protein molecules with three channels is a possible carrier of bio-energy transport and the improved model is possibly a candidate for the mechanism of this transport.     

Properties of Soliton-Transported Bio-energy in α-Helix Protein Molecules with Three Channels

We study numerically the propagating properties of soliton-transported bio-energy excited in the α-helix protein molecules with three channels in the cases of the short-time and long-time motions and its features of collision at temperature T = 0 and biological temperature T = 300 K by the dynamic equations in the improved Davydov theory and fourth-order Runge-Kutta method, respectively. From these simulation experiments we see that the new solitons in the improved model can move without dispersion at a constant speed retaining its shape and energy in the cases of motion of both short-time or T = 0 and long time or T = 300 K and can go through each other without scattering in their collisions. In these cases its lifetime is, at least, 120 ps at 300 K, in which the soliton can travel over about 700 amino acid residues. This result is consistent with analytic result obtained by quantum perturbed theory in this model. In the meanwhile, the influences of structure disorder of α-helix protein molecules, including the inhomogeneous distribution of amino acids with different masses and fluctuations of spring constant, dipole-dipole interaction, exciton-phonon coupling constant and diagonal disorder, on the solitons are also studied by the fourth-order Runge-Kutta method. The results show that the soliton still is very robust against the structure disorders and thermal perturbation of proteins at biological temperature 300 K. Therefore we can conclude that the new soliton in the α-helix protein molecules with three channels is a possible carrier of bio-energy transport and the improved model is possibly a candidate for the mechanism of this transport.     

Influence of structure disorders and temperaturesof systems on the bio-energy transport in proteinmolecules (Ⅱ)

The influence of molecular structure disorders and physiological temperature on the states and properties of solitons as transporters of bio-energy are numerically studied through the fourth-order Runge-Kutta method and a new theory based on my paper [Front. Phys. China, 2007, 2(4): 469]. The structure disorders include fluctuations in the characteristic parameters of the spring constant, dipole-dipole interaction constant and exciton-phonon coupling constant, as well as the chain-chain interaction coefficient among the three channels and ground state energy resulting from the disorder distributions of masses of amino acid residues and impurities. In this paper, we investigate the behaviors and states of solitons in a single protein molecular chain, and in α-Helix protein molecules with three channels. In the former we prove first that the new solitons can move without dispersion, retaining its shape, velocity and energy in a uniform and periodic protein molecule. In this case of structure disorder, the fluctuations of the spring constant, dipole-dipole interaction constant and exciton-phonon coupling constant, as well as the ground state energy and the disorder distributions of masses of amino acid residues of the proteins influence the states and properties of motion of solitons. However, they are still quite stable and are very robust against these structure disorders, even in the presence of larger disorders in the sequence of masses, spring constants and coupling constants. Still, the solitons may disperse or be destroyed when the disorder distribution of the masses and fluctuations of structure parameters are quite great. If the effect of thermal perturbation of the environment on the soliton in nonuniform proteins is considered again, it is still thermally stable at the biological temperature of 300 K, and at the longer time period of 300 ps and larger spacing of 400 amino acids. The new soliton is also thermally stable in the case of motion over a long time period of 300 ps in the region of 300–320 K under the influence of the above structure disorders. However, the soliton disperses in the case of a higher temperature of 325 K and in larger structure disorders. Thus, we determine that the soliton’s lifetime and critical temperature are 300 ps and 300–320 K, respectively. These results are also consistent with analytical data obtained via quantum perturbed theory. In α-Helix protein molecules with three channels, results obtained show that these structure disorders and quantum fluctuations can change the states and features of solitons, decrease their amplitudes, energies and velocities, but they still cannot destroy the solitons, which can still transport steadily along the molecular chains while retaining energy and momentum when the quantum fluctuations are small, such as in structure disorders and quantum fluctuations of and and . Therefore, the solitons in the improved model are quite robust against these disorder effects. However, the solitons may be dispersed or disrupted in cases of very large structure disorders. When the influence of temperature on solitons is considered, we find that the new solitons can transport steadily over 333 amino acid residues in the case of motion over a long time period of 120 ps, and can retain their shapes and energies to travel forward along protein molecules after mutual collision of the solitons at the biological temperature of 300 K. Therefore, the soliton is also very robust against thermal perturbation of the α-helix protein molecules at 300 K. However, the soliton disperses in cases of higher temperatures at 325 K and in larger structure disorders. Thus, their critical temperature is about 320 K. When the effects of structure disorder and temperature are considered simultaneously, the soliton has high thermal stability and can transport for a long time along the protein molecular chains while retaining its amplitude, energy and velocity, even though the fluctuations of the structure parameters and temperature of the medium increase continually. However, the soliton disperses in the larger fluctuations of and at T=300 K, and at temperatures higher than 315 K when the fluctuations are and . This means that the critical temperature of the soliton is only 315 K in this condition. In a word, we can conclude from the above investigations that the soliton in the improved model is very robust against the structure disorders and thermal perturbation of proteins at the biological temperature of 300 K in α-helix protein molecules, and is a possible bio-energy transport carrier; the improved model is a possible candidate for the mechanism of this transport.      

Impact of Slip Cycles on the Operation Modes and Efficiency of Molecular Motors

Kinesin is a motor molecule that moves processively on microtubule tracks and is involved in active intracellular transport processes. For small loads, it is powered by the hydrolysis of one ATP molecule per step. Here we extent our previously introduced network theory in order to study the possibility of two different mechanical stepping transitions and the general behavior of the motor’s efficiency. Our theory shows explicitly how chemical and mechanical slip cycles emerge that weaken the coupling between ATP hydrolysis and mechanical stepping. Near chemomechanical equilibrium, the motor efficiency η may vary between η=1 for tight coupling and η=0 for loose coupling, depending on the relevance of the slip cycles. Far from chemomechanical equilibrium, on the other hand, the motor efficiency is found to decay as 1/Δμ with increasing Δμ irrespective of the presence of slip cycles, where Δμ represents the reaction free enthalpy or chemical potential difference per ATP hydrolysis.     

Weak Coupling and Continuous Limits for Repeated Quantum Interactions

We consider a quantum system in contact with a heat bath consisting in an infinite chain of identical sub-systems at thermal equilibrium at inverse temperature β. The time evolution is discrete and such that over each time step of duration τ, the reference system is coupled to one new element of the chain only, by means of an interaction of strength λ. We consider three asymptotic regimes of the parameters λ and τ for which the effective evolution of observables on the small system becomes continuous over suitable macroscopic time scales T and whose generator can be computed: the weak coupling limit regime λ → 0, τ = 1, the regime τ → 0, λ²τ → 0 and the critical case λ²τ = 1, τ → 0. The first two regimes are perturbative in nature and the effective generators they determine is such that a non-trivial invariant sub-algebra of observables naturally emerges. The third asymptotic regime goes beyond the perturbative regime and provides an effective dynamics governed by a general Lindblad generator naturally constructed from the interaction Hamiltonian. Conversely, this result shows that one can attach to any Lindblad generator a repeated quantum interactions model whose asymptotic effective evolution is generated by this Lindblad operator.     

Huygens' Principle,Dirac Operators,and Rational Solutions of the AKNS Hierarchy

We prove that rational solutions of the AKNS hierarchy of the form q=σ/τ and r=ρ/τ, where (σ,τ,ρ) are certain Schur functions, naturally yield Dirac operators of strict Huygens' type, i.e., the support of their fundamental solutions is the surface of the light-cone. This strengthens the connection between the theory of completely integrable systems and Huygens' principle by extending to the Dirac operators and the rational solutions of the AKNS hierarchy a classical result of Lagnese and Stellmacher concerning perturbations of wave operators. Mathematics Subject Classifications (2000) 37K10, 35Qxx, 35B40.     

Influence of structure disorders and temperatures of systems on the bio-energy transport in protein molecules (II)

The influence of molecular structure disorders and physiological temperature on the states and properties of solitons as transporters of bio-energy are numerically studied through the fourth-order Runge-Kutta method and a new theory based on my paper [Front. Phys. China, 2007, 2(4): 469]. The structure disorders include fluctuations in the characteristic parameters of the spring constant, dipole-dipole interaction constant and exciton-phonon coupling constant, as well as the chain-chain interaction coefficient among the three channels and ground state energy resulting from the disorder distributions of masses of amino acid residues and impurities. In this paper, we investigate the behaviors and states of solitons in a single protein molecular chain, and in α-Helix protein molecules with three channels. In the former we prove first that the new solitons can move without dispersion, retaining its shape, velocity and energy in a uniform and periodic protein molecule. In this case of structure disorder, the fluctuations of the spring constant, dipole-dipole interaction constant and exciton-phonon coupling constant, as well as the ground state energy and the disorder distributions of masses of amino acid residues of the proteins influence the states and properties of motion of solitons. However, they are still quite stable and are very robust against these structure disorders, even in the presence of larger disorders in the sequence of masses, spring constants and coupling constants. Still, the solitons may disperse or be destroyed when the disorder distribution of the masses and fluctuations of structure parameters are quite great. If the effect of thermal perturbation of the environment on the soliton in nonuniform proteins is considered again, it is still thermally stable at the biological temperature of 300 K, and at the longer time period of 300 ps and larger spacing of 400 amino acids. The new soliton is also thermally stable in the case of motion over a long time period of 300 ps in the region of 300–320 K under the influence of the above structure disorders. However, the soliton disperses in the case of a higher temperature of 325 K and in larger structure disorders. Thus, we determine that the soliton’s lifetime and critical temperature are 300 ps and 300–320 K, respectively. These results are also consistent with analytical data obtained via quantum perturbed theory. In α-Helix protein molecules with three channels, results obtained show that these structure disorders and quantum fluctuations can change the states and features of solitons, decrease their amplitudes, energies and velocities, but they still cannot destroy the solitons, which can still transport steadily along the molecular chains while retaining energy and momentum when the quantum fluctuations are small, such as in structure disorders and quantum fluctuations of $ 0.67 < \alpha _k < 2,\Delta W = \pm 8\% \overline W ,\Delta J = \pm 1\% \overline J ,\Delta (\chi _1 + \chi _2 ) = \pm 3\% (\bar \chi _1 + \bar \chi _2 ) $ and $ \Delta L = \pm 1\% \bar L $ and $ \Delta \varepsilon _0 = \varepsilon \left| {\beta _n } \right|,\varepsilon = 0.1 meV,\left| {\beta _n } \right| < 0.5 $ . Therefore, the solitons in the improved model are quite robust against these disorder effects. However, the solitons may be dispersed or disrupted in cases of very large structure disorders. When the influence of temperature on solitons is considered, we find that the new solitons can transport steadily over 333 amino acid residues in the case of motion over a long time period of 120 ps, and can retain their shapes and energies to travel forward along protein molecules after mutual collision of the solitons at the biological temperature of 300 K. Therefore, the soliton is also very robust against thermal perturbation of the α-helix protein molecules at 300 K. However, the soliton disperses in cases of higher temperatures at 325 K and in larger structure disorders. Thus, their critical temperature is about 320 K. When the effects of structure disorder and temperature are considered simultaneously, the soliton has high thermal stability and can transport for a long time along the protein molecular chains while retaining its amplitude, energy and velocity, even though the fluctuations of the structure parameters and temperature of the medium increase continually. However, the soliton disperses in the larger fluctuations of $ 0.67\overline M < M_k < 2\overline M , \Delta (\chi _1 + \chi _2 ) = \pm 2\% (\bar \chi _1 + \bar \chi _2 ), \Delta J = \pm 1.3\% \bar J, \Delta W = \pm 6\% \overline W , \Delta L = \pm 1.5\% \overline L $ and $ \Delta \varepsilon _0 = \varepsilon \left| {\beta _n } \right|, \varepsilon = 0.82 meV, \left| {\beta _n } \right| \leqslant 0.5 $ at T=300 K, and at temperatures higher than 315 K when the fluctuations are $ 0.67\overline M < M_k < 2\overline M , \Delta (\chi _1 + \chi _2 ) = \pm 1\% (\bar \chi _1 + \bar \chi _2 ), \Delta J = \pm 0.7\% \bar J, \Delta W = \pm 7\% \overline W , \Delta L = \pm 0.8\% \overline L $ and $ \Delta \varepsilon _0 = \varepsilon \left| {\beta _n } \right|, \varepsilon = 0.4 meV, \left| {\beta _n } \right| \leqslant 0.5 $ . This means that the critical temperature of the soliton is only 315 K in this condition. In a word, we can conclude from the above investigations that the soliton in the improved model is very robust against the structure disorders and thermal perturbation of proteins at the biological temperature of 300 K in α-helix protein molecules, and is a possible bio-energy transport carrier; the improved model is a possible candidate for the mechanism of this transport.     

On the Point-Particle (Newtonian) Limit¶of the Non-Linear Hartree Equation

We consider the nonlinear Hartree equation describing the dynamics of weakly interacting non-relativistic Bosons. We show that a nonlinear M?ller wave operator describing the scattering of a soliton and a wave can be defined. We also consider the dynamics of a soliton in a slowly varying background potential W(ɛx). We prove that the soliton decomposes into a soliton plus a scattering wave (radiation) up to times of order ɛ⁻¹. To leading order, the center of the soliton follows the trajectory of a classical particle in the potential W(ɛx). Received: 30 June 2000 / Accepted: 25 June 2001     

On the theory of chirped optical solitons in fiber lines with varying dispersion

We study a soliton solution of a path-averaged (in the spectral domain) propagation equation governing the transmission of a chirped breather pulse in the fiber lines with dispersion compensation. We demonstrate that the averaged Hamiltonian model correctly describes features of the chirped soliton observed in numerical simulations and experiments. We show that the Hamiltonian is bounded from below if the average dispersion is anomalous 〈 d〉>0); that, together with the condition H _sol<0, indicates stability of dispersion-managed solitons in this region. Pis’ma Zh. éksp. Teor. Fiz. 68, No. 11, 791–795 (10 December 1998) Published in English in the original Russian journal. Edited by Steve Torstveit.     

Symmetry of nuclear Hamiltonian as an origin of clustering

It is established that the set of solutions of the Hamiltonian of the generalized Elliott SU(3) model in the space of A-fermion wave functions contains a subset of multicluster solutions Ψ_Δ ^A which can be precisely represented in terms of solutions of the Hamiltonian of the same form acting in the reduced space of certain intercluster coordinates. The conditions imposed on a multicluster partition which exhibits such properties are determined by applying the group-theory methods.     

A Molecular Dynamical Theory of Ultraweak Bio－photon Emission in the LivingSystems and Its Propertes（1）

ＡＭｏｌｅｃｕｌａｒＤｙｎａｍｉｃａｌＴｈｅｏｒｙｏｆＵｌｔｒａｗｅａｋＢｉｏ－ｐｈｏｔｏｎＥｍｉｓｓｉｏｎｉｎｔｈｅＬｉｖｉｎｇＳｙｓｔｅｍｓａｎｄＩｔｓＰｒｏｐｅｒｔｅｓ（１）￥ＰａｎｇＸｉａｏｆｅｎｇ（ＩｎｔｅｒｎａｔｉｏｎａｌＣｅｎｔｒｅｆｏ...     

Doubly Periodic Wave Solutions and Soliton Solutions of Ablowitz–Ladik Lattice System

The general Jacobi elliptic function expansion method is developed and extended to construct doubly periodic wave solutions for discrete nonlinear equations. Applying this method, many exact elliptic function doubly periodic wave solutions are obtained for Ablowitz–Ladik lattice system. When the modulus m→1 or m→0, these solutions degenerate into hyperbolic function solutions and trigonometric function solutions respectively. In long wave limit, solitonic solutions including bright soliton and dark soliton solutions are also obtained.     

KdV-soliton dynamics in a random field

We consider the interaction between soliton and a spatially uniform external random field within the framework of the forced Korteweg-de Vries equation. In the general case, the averaged soliton field is transformed to a Gaussian pulse whose amplitude falls off with time as t^−α, while its width increases as t^α, where the parameter α is characterized by the statistical properties of the external force. We obtain an analytical solution for α = 2, which corresponds to the limiting case of an infinitely long correlation time (τ₀ → ∞). The obtained solution is compared with the well-known Wadati solution for the case of a delta-correlated external force (τ₀ → 0) where the soliton is transformed to a Gaussian pulse with amplitude falling off at a lower rate α = 3/2. The numerical solutions of the forced Korteweg-de Vries equation, which demonstrate an increase in the parameter α from 3/2 to 2 with increasing correlation time, are given for the intermediate case corresponding to 0 < τ₀ < ∞. It is shown that the amplitude of the averaged soliton in a periodic random field falls off as t⁻¹ for the long times t. In this case, two pulses propagating in different directions are formed. __________ Translated from Izvestiya Vysshikh Uchebnykh Zavedenii, Radiofizika, Vol. 49, No. 7, pp. 599–606, July 2006.