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

Jaeken, Laurent

doi:10.1016/j.pbiomolbio.2017.03.002

Cited by 20 publications

(9 citation statements)

References 82 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…186 Additionally, it was recently hypothesized that spaces between mica sheets may have been potential sites for the origin of life, as they may have provided shelters to the primitive PMLOs. 187 Taken together, these examples underscore the critical role of IDPs in life's origin and evolution on the earth, 188 which ultimately led to the evolution of multicellular forms and their expansion.…”

Section: Idps and Prebiotic Evolutionmentioning

confidence: 99%

Intrinsically Disordered Proteins: Critical Components of the Wetware

et al. 2022

View full text Add to dashboard Cite

Despite the wealth of knowledge gained about intrinsically disordered proteins (IDPs) since their discovery, there are several aspects that remain unexplored and, hence, poorly understood. A living cell is a complex adaptive system that can be described as a wetwarea metaphor used to describe the cell as a computer comprising both hardware and software and attuned to logic gatescapable of “making” decisions. In this focused Review, we discuss how IDPs, as critical components of the wetware, influence cell-fate decisions by wiring protein interaction networks to keep them minimally frustrated. Because IDPs lie between order and chaos, we explore the possibility that they can be modeled as attractors. Further, we discuss how the conformational dynamics of IDPs manifests itself as conformational noise, which can potentially amplify transcriptional noise to stochastically switch cellular phenotypes. Finally, we explore the potential role of IDPs in prebiotic evolution, in forming proteinaceous membrane-less organelles, in the origin of multicellularity, and in protein conformation-based transgenerational inheritance of acquired characteristics. Together, these ideas provide a new conceptual framework to discern how IDPs may perform critical biological functions despite their lack of structure.

show abstract

Section: Idps and Prebiotic Evolutionmentioning

confidence: 99%

Intrinsically Disordered Proteins: Critical Components of the Wetware

et al. 2022

View full text Add to dashboard Cite

show abstract

“…This, in turn, can lead to polarization of the associated and structured water layers. The resulting fractal "cell matrix'' supports coherent vibrations and harmonic resonance and may induce bio-photon discharge that can produce holographic properties (reviewed in [141] [142]).…”

Section: Steering By Holographic Memory Hypersphere Of the Individualmentioning

confidence: 99%

Guided Folding of Life’s Proteins in Integrate Cells with Holographic Memory and GM-Biophysical Steering

Meijer¹,

Geesink²

2018

OJBIPHY

View full text Add to dashboard Cite

The current geometric and thermodynamic approaches in protein folding studies do not provide a definite solution to understanding mechanisms of folding of biological proteins. A major problem is that the protein is first synthesized as a linear molecule that subsequently must reach its native configuration in an extremely short time. Hydrophobicity-hydrophilicity models and random search mechanism cannot explain folding to the 3-D functional form in less than 1 second, as it occurs in the intact cell. We propose an integral approach, based on the embedding of proteins in the whole cellular context under the postulate: a life protein is never alone. In this concept the protein molecule is influenced by various long and short distance force fields of nature such as coherent electromagnetic waves and zero-point energy. In particular, the role of solitons is reviewed in relation to a novel GM-scale biophysical principle, revealed by us. This recent finding of a set of discrete EM frequency bands, that either promote or endanger life conditions, could be a key in further studies directed at the morphogenetic aspects of protein folding in a biological evolutionary context. In addition, an alternative hypothesis is presented in which each individual cell may store integral 3-D information holographically at the virtual border of a 4-D hypersphere that surrounds each living cell, providing a field receptive memory structure that is instrumental in guiding the folding process towards coherently oscillating protein networks that are crucial for cell survival.(hydrophobic-hydrophilic) model, is extremely complex (i.e., generally requires an enormous number of steps [2]. Levinthal concluded rightfully that a random search can only be performed in an unrealistic timeframe of billions of years [1]. Thus two major questions remain: what are the actual folding mechanisms and how can this ultra-rapid process be realized in the whole, intact, cell structure?Martinez noted that the current folding models had weak predictive ability [3]. Natural proteins consist of 100 to 500 building blocks (alpha-amino-acids), but a random search mechanism cannot provide real-time folding on the order of 1 sec. for these proteins. In the framework of a funnel-like energy landscape, the author considers a simple kinetic model of protein folding. However, this kinetic model assumes that once a domain reaches the correct state, it stays there. However, it remains unclear how the domain "knows" that it reached the correct state. After all, an intermediate state is not the minimum energy a state-the minimum is only expected for the whole structure. In the current geometric and thermodynamic approaches in protein folding mechanisms, impressive progress was made, as for instance exemplified by recent papers [4] [5], yet such bottom up approaches fail to provide a satisfactory and generally predictive solution.Munoz and Cerminara recently reviewed current generation of thermodynamic methods to map ultrafast folding landscapes, interaction networks and var...

show abstract

“…In the AIH, a protein exhibiting extended conformations is called an extroverted system, and is more likely to H-bond and polarize the surrounding water, altering its properties (such as its relaxation dynamics, viscoelasticity, solvency). Examples are proteins forming fibrillar structures (such as actin and tubulin) or proteins displaying a high contribution of random coil conformations, such as the intrinsically disordered proteins [5,69]. From these two components of the AIH (i.e., association and induction) a unified theory of cellular activity emerges [70].…”

Section: The Association-induction Hypothesis (Aih) Intracellular Wat...mentioning

confidence: 99%