Dynamic Kinetic Stability

Author(s):  
Addy Pross
2005 ◽  
Vol 77 (11) ◽  
pp. 1905-1921 ◽  
Author(s):  
Addy Pross

Despite the considerable advances in our understanding of biological processes, the physicochemical relationship between living and nonliving systems remains uncertain and a continuing source of controversy. In this review, we describe a kinetic model based on the concept of dynamic kinetic stability that attempts to incorporate living systems within a conventional physicochemical framework. Its essence: all replicating systems, both animate and inanimate, represent elements of a replicator space. However, in contrast to the world of nonreplicating systems (all inanimate), where selection is fundamentally thermodynamic, selection within replicator space is effectively kinetic. As a consequence, the nature of stability within the two spaces is of a distinctly different kind, which, in turn, leads to different physicochemical patterns of aggregation. Our kinetic approach suggests: (a) that all living systems may be thought of as manifesting a kinetic state of matter (as apposed to the traditional thermodynamic states associated with inanimate systems), and (b) that key Darwinian concepts, such as fitness and natural selection, are particular expressions of more fundamental physicochemical concepts, such as kinetic stability and kineticselection. The approach appears to provide an improved basis for understanding the physicochemical process of complexification by which life on earth emerged, as well as a means of relating life's defining characteristics - its extraordinary complexity, its far-from-equilibrium character, and its purposeful (teleonomic) nature - to the nature of that process of complexification.


2021 ◽  
Vol 5 (3) ◽  
Author(s):  
Sachin V. Muley ◽  
Chengrong Cao ◽  
Debaditya Chatterjee ◽  
Carter Francis ◽  
Felix P. Lu ◽  
...  

2021 ◽  
Vol 167 ◽  
pp. 405-414
Author(s):  
Zhemin Liu ◽  
Qingping Liang ◽  
Peng Wang ◽  
Qing Kong ◽  
Xiaodan Fu ◽  
...  

2021 ◽  
Vol 1233 ◽  
pp. 130079
Author(s):  
Akbar Hassanpour ◽  
Leila Youseftabar-Miri ◽  
Parvaneh Delir Kheirollahi Nezhad ◽  
Sheida Ahmadi ◽  
Saeideh Ebrahimiasl

1984 ◽  
Vol 224 (2) ◽  
pp. 577-580 ◽  
Author(s):  
M Madden ◽  
S M Lau ◽  
C Thorpe

Pig kidney general acyl-CoA dehydrogenase is markedly stabilized against loss of flavin and activity in 7.3 M-urea or at 60 degrees C upon reduction with sodium dithionite or octanoyl-CoA. Electron transferring flavoprotein is similarly stabilized, whereas egg white riboflavin-binding protein loses flavin more readily on reduction. These and other data support the anticipated correlation between the kinetic stability of the holoproteins and the oxidation-reduction potential of their bound flavins.


2016 ◽  
Vol 432 ◽  
pp. 95-101 ◽  
Author(s):  
Lance M. Hellman ◽  
Liusong Yin ◽  
Yuan Wang ◽  
Sydney J. Blevins ◽  
Timothy P. Riley ◽  
...  

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