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The evolutionary origin of sensorimotor control requires a sort of physical durability, other than Galilean inertia being accessible in third-person description in the present tense. One candidate to address this need is the 'class property' of a material body's durability remaining invariant during the exchange of component elements. Using grammatical tense as a descriptive attribute, this durability is accessible only in the frequent update of the present perfect tense in the present progressive tense at the 'now' of the present moment. In this view, the update of the perfect tense is equated with the onset and occurrence of on/off switching behavior of physical origin underlying the phenomena of sensorimotor control. Notably, the physical update of the perfect tense is specific only to the 'now and here' that is central in the tradition of phenomenology. The phenomena upholding thermodynamics, when taken apart from its theory, are decisive in facilitating the onset of sensorimotor control. Instrumental to the emergence of both life in general and sensorimotor control in particular may be the occurrence of a 'physical and chemical affinity' of the material bodies of whatever type. Such will let the constant exchange of component elements be feasible, so that the class identity equipped with the capacity for measurement is made available within the phenomenon. Material bodies constantly exchanging such component elements would make the material world open to biology by allowing each element to experience the organizational whole from within. The internal observer responsible for the origins of life may do double duty of letting itself be durable on the material basis while observing the conditions making it durable on the linguistic ground. The origins of life appear to us a material phenomenon when they are approached with use of our linguistic tools that can get rid of the strict stipulation of an abstract nature applied to the description of dynamical laws in physics.

A reaction cycle in general or a metabolic cycle in particular owes its evolutionary emergence to the covering reaction environment acting as a measurement apparatus of a natural origin. The quantum measurement of the environmental origin underlying the molecular processes observed in the biological realm is operative cohesively between the measuring and the measured. The measuring part comes to pull in a quantum as an indivisible lump available from an arbitrary material body to be measured. The inevitable difference between the impinging quantum upon the receiving end on the part of the environment and the actual quantum pulled into the receiving end comes to effectively be nullified through the retrocausative propagation of the corresponding wave function proceeding backwards in time. The retrocausal regulation applied to the interface between the measuring and the measured is to function as the organizational agency supporting biology, and is sought in the act for the present in the immediate future within the realm of quantum phenomena. Molecular dynamics in biology owes both the evolutionary buildup and maintenance of its organization to the retrocausal operation of the unitary transformation applied to quantum phenomena proceeding backwards in time. Quantum measurement provides the cohesive agency that is pivotal for implementing the retrocausal regulation. In particular, the physical origin of Darwinian natural selection can be seen in the retrocausal regulation applied to the unitary transformation of a quantum origin.

Fourier's law of heat transfer addressing temperature differences is intrinsically selective in favoring the mitigation of the differences proceeding as fast as possible. We present an experimental demonstration of such selective behavior of material origin. When an actin filament equipped with nano-scale heat acceptors was placed under heat pulsation, it demonstrated a unidirectional movement without the presence of myosin or ATP. The prime factor for the unidirectional movement was the temperature differences between the locally heated portions on the actin filament and the cooler material bodies in the surroundings. The unidirectional movement could be enhanced in the process of mitigating the temperature differences as fast as possible.

An ATP-activated actin filament sliding on myosin molecules exhibited mechanical distortions or fluctuations both longitudinally and transversally along the filament. Although actin filaments exhibited a uniform sliding movement longitudinally as the ATP concentration increased, the longitudinal fluctuations were found to vary their magnitude with the concentration. The magnitude of longitudinal fluctuations reached its maximum at approximately 100 microM of the ATP concentration. The local enhancement of the longitudinal fluctuations as responding to changes in the ATP concentration is associated with a critical phenomenon bridging the two different kinds of mechanical distortions, either contractile or protractile ones, occurring within a sliding actin filament.

The sliding velocity of actin filaments was found to increase in the presence of ATP analogues. At 0.5 mM ATP, the presence of 2.0 mM of AMP-PNP enhanced the filament velocity from 3.2 up to 4.5 microm/s. However, 2 mM ADP decreased the velocity down to 1.1 microm/s. The results suggest that the complex conformations of myosin cross-bridges interacting with an actin filament in the presence of ATP analogues makes the entire filament move faster.

Oligomerization of amino acids proceeded on or inside lipid vesicles as a model of prebiotic cells in a simulated hydrothermal environment. When the suspension of lipid vesiclestaking up monomeric glycine underwent a sudden temperature dropby traversing from a hot (180 °C) to a cold (0 °C) region repeatedly while circulating through a closedreaction circuit, oligopeptides up to heptaglycine were formed even in the absence of condensing agents.

An actin filament sliding on myosin moleculesdemonstrates both longitudinal distortions and transversal fluctuationswith the linear dimension far exceeding the diameter of an actinmonomer. Local swaying of a single actin filament was identified byreading speckled fluorescent markers attached on the filament. Theaccuracy of reading each speckled marker was about 10.4 nm (r.m.s.).Longitudinal distortions of an actin filament at a low ATP concentrationof 20 μM were as much as 0.5 μm for the average filament lengthof 5.4 μm. The magnitude of transversal fluctuations was as much as60 nm, that was independent of the filament length. Both longitudinaldistortions and transversal fluctuations are suggested to play a pivotalrole for facilitating a smooth sliding movement of an actin filament.

An actin filament contacting myosin molecules increased the fluctuation intensity of the filamental displacement as the ATP concentration increased. In particular, fluctuations in the filamental displacement in the planar plane in which the sliding movement takes place were isotropic at a low ATP concentration, and became anisotropic as the concentration increased. The build-up of the sliding movement of an actin filament was associated with the transformation from isotropic to anisotropic fluctuations of the filamental displacement.

An actin filament exhibits distortions longitudinally when it slides upon myosin molecules. We observed that the actin filament demonstrated contractile distortions at low ATP concentrations and protractile distortions at high concentrations. Temporal development of such distortions was identified, by tracing each of several speckled fluorescent markers attached to the actin filament. Close association of the sliding movement to the moving distortions of an actin filament suggests the presence of a unitary mechanism regulating the apparently two different modes of dynamic movement.

Cell motility underlying muscle contraction is imputed to a macroscopic quantum mechanical coherence actualized locally in the body of a biological organism. Actin-activated myosin ATPase activity functions as a heat sink operating effectively at an extremely low temperature. Extraction of heat energy from the actin filament can help condensing the atomic degrees of freedom constituting the filament into a macroscopic quantum state carrying a nonvanishing linear momentum. Sliding movement of an actin filament on myosin molecules while hydrolyzing ATP molecules is a consequence of the quantum mechanical coherence due to an extremely slow release of energy stored in an ATP molecule.

An actin filament sliding on myosin molecules in the presence of an extremely low concentration of ATP exhibited a staggered movement. Longitudinally sliding movement of the filament was frequently interrupted by its non-sliding, fluctuating movements both in the longitudinal and transversal directions. Intermittent sliding movements of an actin filament indicate establishment of a coordination of ATP-mediated active sites distributed along the filament.

All of the basic functional components of living organisms participating in describing, translating and constructing themselves are described deep within the supporting dynamics itself. A most common material vehicle for implementing this type of self-organization is a material vehicle holding its own identity through the constant exchange of the constituent material elements. The exchange of materials serves as a material means for temporarily ameliorating the infliction of vicious circles being inevitable and latent in the self-referential complications when descriptively approached in the present tense alone, thus dissolving the difficulties in making their predication logically transparent on material terms. Since the exchange of materials is demonstrable experimentally as in the running of the citric acid cycle in the absence of biological enzymes under the conditions simulating the prebiotic environments in the vicinity of hydrothermal vents on the primitive ocean floor, the prior emergence of metabolism could make the subsequent emergence of metabolism-replication complex more likely compared to the cases otherwise. An essence of the occurrence of the material vehicle holding its identity through the exchange of reacting molecules with the new ones recruited from the outside is in the soundness of internalizing the description of the dynamics into the dynamics itself, which is approachable through the constant update of the present perfect tense in the present progressive tense.

Myosin molecules contacting an actin filament in the presence of ATP were found to regulate the filamental fluctuations due to ATP hydrolysis in a communicative manner along the filament. As an evidence of the occurrence of the communication, ATP-activated fluctuating displacements of the filament in the direction perpendicular to its longitudinal axis were identified to propagate at a finite velocity not less than about 0.2 micron/s unidirectionally along the filament.

A comparison was made between fluctuations in a length of sarcomere from a myofibril during relaxed and rigor conditions. The fluctuations of the length associated with rigor states was due entirely to thermal fluctuations in the ambient. In contrast, the fluctuations associated with relaxed states were accompanied by extremely slow and macroscopically modulated thermal fluctuations. A slow, macroscopic modulation of the thermal fluctuations of the length of sarcomere was found to be unique to myofibrils in their relaxed conditions.

Although Oparin used coacervate droplets from two or more types of polymer to model the first cell, he hypothesized homacervation from protein, consistent with Pasteur and Darwin. Herrera made two amino acids and numerous cell-like structures (“sulfobes”) in the laboratory, which probably arose from intermediate polymers. Our experiments have conformed with a homoacervation of thermal proteinoid, in which amino acid sequences are determined by the reacting amino acids themselves. All proteinoids that have been tested assemble themselves alone in water to protocells. The protocells have characteristics of life defined by Webster's Dictionary: metabolism, growth, reproduction and response to stimuli in the environment. The protocells are able also to evolve to more modern cells including the initiation of a nucleic acid coding system.

The emergence of the first cellular organization on the primitive earth could be associated with pronounced heterotrophic activity embodied in heat engines actualized in local material aggregates. Heterotrophic activity intrinsically rests upon the capacity of local detection upholding the conservation of energy on the global scale.

We examined both longitudinal and transversal fluctuations of displacements of an actin filament sliding upon Chara myosin molecules. Although the magnitude of transversal fluctuations remained rather independent of ATP concentration, the longitudinal ones were found to increase their magnitude as the concentration increased. In addition, the longitudinal fluctuations gradually increased as the sliding velocity of the filament increased.

Dynamics without boundary conditions has been attempted to address an extreme subtlety of what looks like boundary conditions or constraints appeared in the biological realm. Microdynamic context accessible in first- and second-person descriptions in the present progressive tense can precipitate the robust macrodynamic data, that are retroactively couched upon the standard dynamics supplemented by specific boundary conditions framed in third-person descriptions in the present tense. Addressing dynamics in first- and second-person descriptions grounds itself upon the process of measurement internal to any material bodies. Internal measurement comes to provide a material means for naturalizing both consciousness and attentive awareness.

The moving velocities of vesicles in the cytoplasmic streaming of a slime mold were measured, in which all of the vesicles passing through a designated window were counted. Vesicles in the streaming are distributed in their moving velocities and the distribution itself varies with time. The mean velocity of vesicles and its standard deviation were found to exhibit a linear relationship, suggesting a possibility that vesicles in the cytoplasm would also be involved in force generation.

Troponin-tropomyosin complex from skeletal muscles was observed to regulate sliding movement of actin filaments on myosin molecules in a manner independent of their ATPase activity. When actin molecules were crosslinked with DSS (disuccinimidyl suberate), the myosin ATPase activity in the presence of the modified actin filaments complexed with both troponin and tropomyosin was only 10% less than that in the case of unmodified actin, and the ATPase activation was independent of calcium ions. In contrast, the sliding velocity of the modified actin filaments on myosin molecules decreased to zero below pCa 6.5. The present results indicate that troponin-tropomyosin complex regulates contractile movement of actomyosin systems through direct alternation of a mechanochemical property of the thin filaments, not through a decrease in the ATPase activity of the myosin molecules.

Single filaments of actin were observed to fluctuate in the direction perpendicular to their longitudinal axes when they hydrolyzed ATP in the presence of myosin. The transversal fluctuations of actin filaments were identified by reading the transversal displacements of the filaments under a fluorescence microscope. The transversal fluctuations in the absence of ATP decreased their intensity as the number of myosin molecules contacting directly with actin filaments increased. In the presence of ATP, on the other hand, the amplitude of the transversal fluctuations increased in proportion to the ATP concentration up to a certain level, while the sliding velocity of the filaments did not increase significantly over the same range of ATP concentration. The present observation suggests that the chemical energy released from ATP along actin filament binding to myosin molecules is first and primarily converted into kinetic energy of fluctuations in the form of the displacement movements of the filaments in the direction perpendicular to their longitudinal axes.

We measured both the ATPase activity of actomyosin complex and the sliding velocity of actin filaments on myosin heads under hydrophobic conditions in the presence of ethanol. Both the ATPase activity and the sliding velocity decrease with the increase of ethanol concentration, if the ionic strength is not too high. As ionic strength increases, there appears an optimum concentration of ethanol that can enhance both the ATPase activity and the sliding velocity.

Actin filaments copolymerized with both intact and chemically modified actin monomers restored their sliding activity when they were supplemented with tropomyosin extracted from skeletal muscle. In contrast, the ATPase activation of the copolymers was decreased when supplemented with tropomyosin. The results indicate that tropomyosin along with actin monomers may facilitate sliding activity of the entire actin filament but suppress ATPase activation of intact actin monomers themselves. Accordingly, tropomyosin molecules could be viewed as playing a dual role of both mechanical and chemical regulation of actin monomers.

A theoretical model is presented for the self-instructing polymerization of free amino acids which proceeds inside microsystems which are phase-separated from the solution of thermal polyamino acids. It is shown theoretically that a compartmentalized microsystem fixes inside itself only the process with a faster macromolecular multiplication as time passes, even if the catalytic polymerization alone could spontaneously decrease the corresponding reaction rate. The compartmentalized machinery of macromolecular multiplication cannot reach its stationary state. The machinery is inevitably multiplied and alternates with those with either faster rates of macromolecular multiplication or slower rates of macromolecular degradation during their time development. These results are based upon the dynamic process that any material system acts by itself so as to remove any flow disequilibrium, that is, to maintain the continuity of material flow.

Thermal proteins arising from the self-sequencing of amino acids satisfy the necessary conditions required for them to become a candidate of the evolutionary precursors of contemporary proteins. The source matrix of information or, equivalently, the statistical ensemble of polypeptides, in reference to which the information content of each amino acid residue can be defined and determined, changes with time endogenously through the production of and the change in the mechanism of production of polypeptides. The change proceeds in the direction along which the order of autocatalysis, the number of autocatalytic polymers needed for synthesizing one such polymer, increases. The underlying dynamics is material flow equilibration working in any material aggregate open to material flow, saying that any open system changes its interaction with the exterior endogenously and successively so as to maintain the continuity of material flow there. The self-sequencing and the autocatalytic polymerization of amino acids are the forms of producing polypeptides. The change in the mechanism of producing polypeptides results from the incorporation of polynucleotides into the polypeptide synthesis. The earlier polymeric information translation proceeds from polypeptide to polynucleotide. The direction of translation is reversed at a later stage of evolution. All these evolutionary events are consistent with viewing thermal proteins produced by self-sequencing of amino acids as an evolutionary precursor of contemporary proteins.