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Native aggregation as a cause of origin of temporary cellular structures needed for all forms of cellular activity, signaling and transformations

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TLDR
According to the hypothesis explored in this paper, native aggregation is genetically controlled (programmed) reversible aggregation that occurs when interacting proteins form new temporary structures through highly specific interactions.
Abstract
According to the hypothesis explored in this paper, native aggregation is genetically controlled (programmed) reversible aggregation that occurs when interacting proteins form new temporary structures through highly specific interactions. It is assumed that Anfinsen's dogma may be extended to protein aggregation: composition and amino acid sequence determine not only the secondary and tertiary structure of single protein, but also the structure of protein aggregates (associates). Cell function is considered as a transition between two states (two states model), the resting state and state of activity (this applies to the cell as a whole and to its individual structures). In the resting state, the key proteins are found in the following inactive forms: natively unfolded and globular. When the cell is activated, secondary structures appear in natively unfolded proteins (including unfolded regions in other proteins), and globular proteins begin to melt and their secondary structures become available for interaction with the secondary structures of other proteins. These temporary secondary structures provide a means for highly specific interactions between proteins. As a result, native aggregation creates temporary structures necessary for cell activity. "One of the principal objects of theoretical research in any department of knowledge is to find the point of view from which the subject appears in its greatest simplicity." Josiah Willard Gibbs (1839-1903)

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Journal ArticleDOI

Low-molecular-weight metabolite systems chemistry

TL;DR: Low molecular-weight metabolites (LMWMs) as discussed by the authors comprise primary or central and a plethora of intermediary or secondary metabolites, all of which are characterized by a molecular weight below 900 Dalton.
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Cell theory, intrinsically disordered proteins, and the physics of the origin of life.

TL;DR: The evidence is given that the first protocells may have been formed on the basis of intrinsically disordered peptides, and available data on the similarity of the physical properties of cell models and living cells allow the Virchow's postulate to be rephrase as follows.
Journal ArticleDOI

Effects of spermine NONOate and ATP on protein aggregation: light scattering evidences

TL;DR: The ATP effect on protein aggregation was ambiguous: ATP alone had no effect on the protein’s thermal stability but it facilitated protein‘s destabilization in the presence of nitric oxide.
Journal ArticleDOI

The neglected functions of intrinsically disordered proteins and the origin of life.

TL;DR: Ling's theory is a complete quantitative theory with corroborated equations for solute distribution, transport, cell potentials and osmotic behaviour and describing the cell's energy cycle and IDP's are involved in all this.
References
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Book ChapterDOI

A Convergence of Experimental and Theoretical Breakthroughs Affirms the PM theory of Dynamically Structured Cell Water on the Theory’s 40th Birthday

TL;DR: This review begins with a summary of the critical evidence disproving the traditional membrane theory and its modification, the membrane-pump theory – as well as their underlying postulations of free cell water, free cell K+, and ‘native’-proteins being truly native.
Journal ArticleDOI

Birefringence of spermatozoa. II. Form birefringence of bull sperm.

TL;DR: In this article, the influence of solvents of different refractive indices on the observed birefringence was investigated, using a new derivation of the Wiener form bireringence equations which allows direct comparison of Wiener's theory with experimental results.
Journal ArticleDOI

Thermal stability of T2 DNA in situ.

TL;DR: Thermal denaturation experiments were carried out on solutions of formaldehydefixed T2 bacteriophage and purified T2 DNA at low salt concentrations and indicated that the tertiary structure of the internal DNA remains intact even at temperatures up to 20 ° higher than the melting temperature of free DNA under comparable conditions.
Journal ArticleDOI

Birefringence of spermatozoa. I. Birefringence melting of squid, bull, and human sperm nucleoprotein.

TL;DR: In experiments designed to determine the thermal stability and bonding strength of a natural nucleoprotein structure, the loss of birefringence as a function of time and temperature was investigated for both mammalian and nonmammalian sperm nuclei.
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