NDLI: Self-propagating beta-sheet polypeptide structures as prebiotic informational molecular entities: the amyloid world.

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Self-propagating beta-sheet polypeptide structures as prebiotic informational molecular entities: the amyloid world.

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Self-propagating beta-sheet polypeptide structures as prebiotic informational molecular entities: the amyloid world.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Maury, C. P. J.
Description	Country affiliation: Finland Author Affiliation: Maury CP ( Department of Medicine, University of Helsinki, Kasarmikatu 11-13, Helsinki FI-00130, Finland. peter.maury@hus.fi)
Abstract	The idea is advanced that under the extreme earth conditions for ~3.9 billions years ago, protein-based beta-sheet molecular structures were the first self-propagating and information-processing biomolecules that evolved. The amyloid structure of these aggregates provided an effective protection against the harsh conditions known to decompose both polyribonucleotides and natively folded polypeptides. In the prebiotic amyloid world, both the replicative and informational functions were carried out by structurally stable beta-sheet protein aggregates in a prion-like mode involving templated self-propagation and storage of information in the beta-sheet conformation. In this amyloid (protein)-first, hybrid replication-metabolism view, the synthesis of RNA, and the evolvement of an RNA-protein world, were later, but necessary events for further biomolecular evolution to occur. I further argue that in our contemporary DNA<-->RNA-->protein world, the primordial beta-conformation-based information system is preserved in the form of a cytoplasmic epigenetic memory.
File Format	HTM / HTML
ISSN	01696149
Issue Number	2
Journal	Origins of Life and Evolution of Biospheres
Volume Number	39
e-ISSN	15730875
Language	English
Publisher	Springer
Publisher Date	2009-04-01
Publisher Place	Netherlands
Access Restriction	Subscribed
Subject Keyword	Discipline Molecular Biology Discipline Biology Amyloid Chemistry Evolution, Molecular Peptides Models, Molecular Prions Protein Conformation Journal Article
Content Type	Text
Resource Type	Article
Subject	Medicine Ecology, Evolution, Behavior and Systematics Space and Planetary Science

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