PubMed Health⌕ Search

PubMed · 8590220

[Order by hazard].

Abstract

Whether a system evolves under the influence of interactions at distance or because of incoherent displacements, due in particular to thermal agitation, it tends toward a state in which compensation exists between the factors likely to influence the arrangement of its components. This state cannot be a random one. It will, of necessity, present some particularity and therefore a certain order. Thermal agitation randomly brings closer together components between which there exist attractions which tend to form structures. The existence of a simple structure opens up the possibility of formation of more complex structures. It is entirely plausible that elementary structures, sites of chemical exchanges coordinated with the environment, primitive living beings were formed purely by chance. These beings might then have given rise, also strictly by chance, to other more highly developed structures which were sites of more complex phenomena. Due to the inevitable existence of fluctuations, it is normal that beings gradually engendered by generations of different individuals would become ever more complex and increasingly different.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

J Tonnelat. 1995. [Order by hazard].. https://pubmed.ncbi.nlm.nih.gov/8590220/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Specific molecular interactions by force spectroscopy: from single bonds to collective properties.

Interactions involving multiple bonds occur throughout biology, and have distinct properties that are fundamentally different from those present in single bond systems. We have developed a new method to analyse the AFM force measurements in order to extract relevant information and to characterise the interactions involving from single to multiple bonds. Our study reveals a surprising behaviour in the presence of multiple bonds with a high rebinding probability: the mean binding forces increase with decreasing pulling velocity. Such behaviour is different from the force dependence on the loading rate for single bond rupture or existing models for multiple bonds rupture.

Biophysical Phenomena↗

Hydrophobic hydration from small to large lengthscales: Understanding and manipulating the crossover.

Small and large hydrophobic solutes exhibit remarkably different hydration thermodynamics. Small solutes are accommodated in water with minor perturbations to water structure, and their hydration is captured accurately by theories that describe density fluctuations in pure water. In contrast, hydration of large solutes is accompanied by dewetting of their surfaces and requires a macroscopic thermodynamic description. A unified theoretical description of these lengthscale dependencies was presented by Lum, Chandler, and Weeks [(1999) J. Phys. Chem. B 103, 4570-4577]. Here, we use molecular simulations to study lengthscale-dependent hydrophobic hydration under various thermodynamic conditions. We show that the hydration of small and large solutes displays disparate dependencies on thermodynamic variables, including pressure, temperature, and additive concentration. Understanding these dependencies allows manipulation of the small-to-large crossover lengthscale, which is nanoscopic under ambient conditions. Specifically, applying hydrostatic tension or adding ethanol decreases the crossover length to molecular sizes, making it accessible to atomistic simulations. With detailed temperature-dependent studies, we further demonstrate that hydration thermodynamics changes gradually from entropic to enthalpic near the crossover. The nanoscopic lengthscale of the crossover and its sensitivity to thermodynamic variables imply that quantitative modeling of biomolecular self-assembly in aqueous solutions requires elements of both molecular and macroscopic hydration physics. We also show that the small-to-large crossover is directly related to the Egelstaff-Widom lengthscale, the product of surface tension and isothermal compressibility, which is another fundamental lengthscale in liquids.

Biophysical Phenomena↗

Biophysical and pharmacological properties of the voltage-gated potassium current of human pancreatic beta-cells.

Voltage-gated potassium (Kv) currents of human pancreatic islet cells were studied by whole-cell patch clamp recording. On average, 75% of the cells tested were identified as beta-cells by single cell, post-recording RT-PCR for insulin mRNA. In most cells, the dominant Kv current was a delayed rectifier. The delayed rectifier activated at potentials above -20 mV and had a V(1/2) for activation of -5.3 mV. Onset of inactivation was slow for a major component (tau = 3.2 s at +20 mV) observed in all cells; a smaller component (tau = 0.30 s) with an amplitude of approximately 25% was seen in some cells. Recovery from inactivation had a tau of 2.5 s at -80 mV and steady-state inactivation had a V(1/2) of -39 mV. In 12% of cells (21/182) a low-threshold, transient Kv current (A-current) was present. The A-current activated at membrane potentials above -40 mV, inactivated with a time constant of 18.5 ms at -20 mV, and had a V(1/2) for steady-state inactivation of -52 mV. TEA inhibited total Kv current with an IC50 = 0.54 mm and PAC, a disubstituted cyclohexyl Kv channel inhibitor, inhibited with an IC50 = 0.57 microm. The total Kv current was insensitive to margatoxin (100 nm), agitoxin-2 (50 nm), kaliotoxin (50 nm) and ShK (50 nm). Hanatoxin (100 nm) inhibited total Kv current by 65% at +20 mV. Taken together, these data provide evidence of at least two distinct types of Kv channels in human pancreatic beta-cells and suggest that more than one type of Kv channel may be involved in the regulation of glucose-dependent insulin secretion.

Biophysical Phenomena↗