How the First Biopolymers Could have Evolved
In this work, we discuss a possible origin of the first biopolymers with stable unique structures. We suggest that at the prebiotic stage of evolution, long organic polymers had to be compact to avoid hydrolysis and had to be soluble and thus must not be exceedingly hydrophobic. We present an algori...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1996-01, Vol.93 (2), p.839-844 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 93 |
| creator | Abkevich, V. I. Gutin, A. M. Shakhnovich, E. I. |
| description | In this work, we discuss a possible origin of the first biopolymers with stable unique structures. We suggest that at the prebiotic stage of evolution, long organic polymers had to be compact to avoid hydrolysis and had to be soluble and thus must not be exceedingly hydrophobic. We present an algorithm that generates such sequences for model proteins. The evolved sequences turn out to have a stable unique structure, into which they quickly fold. This result illustrates the idea that the unique three-dimensional native structures of first biopolymers could have evolved as a side effect of nonspecific physicochemical factors acting at the prebiotic stage of evolution. |
| doi_str_mv | 10.1073/pnas.93.2.839 |
| format | Article |
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I.</au><au>Gutin, A. M.</au><au>Shakhnovich, E. I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>How the First Biopolymers Could have Evolved</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1996-01-23</date><risdate>1996</risdate><volume>93</volume><issue>2</issue><spage>839</spage><epage>844</epage><pages>839-844</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>In this work, we discuss a possible origin of the first biopolymers with stable unique structures. We suggest that at the prebiotic stage of evolution, long organic polymers had to be compact to avoid hydrolysis and had to be soluble and thus must not be exceedingly hydrophobic. We present an algorithm that generates such sequences for model proteins. The evolved sequences turn out to have a stable unique structure, into which they quickly fold. 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| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1996-01, Vol.93 (2), p.839-844 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pubmed_primary_8570645 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Algorithms Amino acids Biochemistry Biological Evolution Biopolymers Chemistry Evolution Hydrolysis Macromolecules Molecular evolution Monomers Origin of Life Peptides - chemistry Polymers Prebiotics Protein Folding Proteins Space life sciences |
| title | How the First Biopolymers Could have Evolved |
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