scispace - formally typeset
Open AccessJournal ArticleDOI

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

Reads0
Chats0
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)

read more

Content maybe subject to copyright    Report

Citations
More filters
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.
Journal ArticleDOI

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
More filters
Journal Article

The cell in development and heredity

Journal ArticleDOI

The physical state of water in living cell and model systems.

TL;DR: Evidence is collected that water molecules in the close vicinity of proteins and other biologically important macromolecules appear to exist in a physical state different from that of normal water.
Journal ArticleDOI

The cytomatrix: a short history of its study

TL;DR: Cellbiology has now emerged as distinct science, but thecytoplasmicmatrix is still not perceived by allcellbiologists assomethingworthstudying, and the recent period hasitnessed the introduction of phasecontrastmicroscopy, which greatlyfacilitated theobservation oflivingcells.
Journal ArticleDOI

Physics of Proteins

TL;DR: The results accumulated over the years inexorably lead to a unified framework for understanding proteins that predicts the existence of a fixed menu of folds determined by geometry, clarifies the role of the amino acid sequence in selecting the native-state structure from this menu, and explains the propensity for amyloid formation.
Related Papers (5)