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  1. 010 学術雑誌論文
  2. 湯川, 哲之 / YUKAWA, Tetsuyuki

'Reverse chemical evolution': A new method to search for thermally stable biopolymers

https://ir.soken.ac.jp/records/3949
https://ir.soken.ac.jp/records/3949
4c4e13d5-d49f-4adf-b58a-969b6821de24
Item type 学術雑誌論文 / Journal Article(1)
公開日 2013-09-17
タイトル
タイトル 'Reverse chemical evolution': A new method to search for thermally stable biopolymers
タイトル
タイトル 'Reverse chemical evolution': A new method to search for thermally stable biopolymers
言語 en
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
アクセス権
アクセス権 metadata only access
アクセス権URI http://purl.org/coar/access_right/c_14cb
著者 MITSUZAWA, Shigenobu

× MITSUZAWA, Shigenobu

MITSUZAWA, Shigenobu

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YUKAWA, Tetsuyuki

× YUKAWA, Tetsuyuki

YUKAWA, Tetsuyuki

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著者別名 湯川, 哲之

× 湯川, 哲之

湯川, 哲之

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抄録
内容記述タイプ Abstract
内容記述 The primitive sea on Earth may have had high-temperature and high-pressure conditions similar to those in present-day hydrothermal environments. If life originated in the hot sea, thermal stability of the constituent molecules would have been necessary. Thus far, however, it has been reported that biopolymers hydrolyze too rapidly to support life at temperatures of more than 200 °C. We herein propose a novel approach, called reverse chemical evolution, to search for biopolymers notably more stable against thermal decomposition than previously reported. The essence of the approach is that hydrolysis of a protein or functional RNA (m-, t-, r-RNA) at high temperature and high pressure simulating the ancient sea environment may yield thermally stable peptides or RNAs at higher concentrations than other peptides or RNAs. An experimental test hydrolyzing bovine ribonuclease A in aqueous solution at 205 °C and 25 MPa yielded three prominently stable molecules weighing 859, 1030 and 695 Da. They are thermally some tens or hundreds times more stable than a polyglycine of comparable mass. Sequence analyses of the 859- and 1030-Da molecules revealed that they are a heptapeptide and its homologue, respectively, elongated by two amino acids at the N-terminal region, originally embedded as residues 112–120 in the protein. They consist mainly of hydrophobic amino acids.
書誌情報 Origins of Life and Evolution of Biospheres
en : Origins of Life and Evolution of Biospheres

巻 33, 号 2, p. 163-171, 発行日 2003-04
出版者
出版者 SpringerLink
ISSN
収録物識別子タイプ ISSN
収録物識別子 0169-6149
DOI
識別子タイプ DOI
関連識別子 https://doi.org/10.1023/A:1024621729149
関連名称 10.1023/A:1024621729149
権利
権利情報 SpringerLink(The original publication is available at www.springerlink.com)
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