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
Citations
More filters
Journal ArticleDOI
Comparison of fundamental physical properties of the model cells (protocells) and the living cells reveals the need in protophysiology
TL;DR: The time has come to conduct comprehensive research into the fundamental physical properties of protocells and create a new discipline – protocell physiology or protophysiology – which should bring us much closer to solving the problem of the origin of life.
Journal ArticleDOI
Coherent Behavior and the Bound State of Water and K(+) Imply Another Model of Bioenergetics: Negative Entropy Instead of High-energy Bonds.
TL;DR: Ling disproved MT and proposed an alternative based on coherence, showing that rest (R) and action (A) are two different phases of protoplasm with different energy levels.
Journal ArticleDOI
Coagulation, flocculation, and denaturation: a century of research into protoplasmic theories of anesthesia.
TL;DR: This article is a reminder of the prolonged interdisciplinary research effort dedicated to “protoplasmic theories” at a time when attention is increasingly directed toward examining the nature of (un)consciousness as well as noncanonical consequences of anesthetic exposure that are not easily accounted for within conventional pharmacological concepts.
Book ChapterDOI
Protein-Protein Interaction Inhibitors: Case Studies on Small Molecules and Natural Compounds
TL;DR: Many biological functions involve the formation of protein–protein complexes, and the inhibition of this process has garnered significant interest in pharmaceutical research investigating novel therapies for several human diseases.
Journal ArticleDOI
Native aggregation is a common feature among triosephosphate isomerases of different species
Mónica Rodríguez-Bolaños,Héctor Miranda-Astudillo,Edgar Pérez-Castañeda,Diego González-Halphen,Ruy Pérez-Montfort +4 more
TL;DR: The results indicate that all the TIMs studied are capable of forming oligomers of different sizes, which is significant because aggregation of TIM may be important in some of its non-catalytic moonlighting functions, like being a potent food allergen, or in its role associated with Alzheimer’s disease.
References
More filters
Journal ArticleDOI
Principles that Govern the Folding of Protein Chains
TL;DR: Anfinsen as discussed by the authors provided a sketch of the rich history of research that provided the foundation for his work on protein folding and the Thermodynamic Hypothesis, and outlined potential avenues of current and future scientific exploration.
Journal ArticleDOI
Macromolecular crowding: obvious but underappreciated.
TL;DR: Positive results of crowding include enhancing the collapse of polypeptide chains into functional proteins, the assembly of oligomeric structures and the efficiency of action of some molecular chaperones and metabolic pathways.
Journal ArticleDOI
Natively unfolded proteins: a point where biology waits for physics.
TL;DR: Results of this analysis showed that intrinsically unstructured proteins do not possess uniform structural properties, as expected for members of a single thermodynamic entity, and the Protein Quartet model, with function arising from four specific conformations (ordered forms, molten globule, premolten globules, and random coils) is discussed.
Journal ArticleDOI
Intrinsic Disorder and Protein Function
Book
Intrinsically Disordered Proteins
TL;DR: The sequence-structure relationships indicate that disorder is an encoded property, and the predictions strongly suggest that proteins in nature are much richer in intrinsic disorder than are those in the Protein Data Bank.