Literature DB >> 23345793

Correlated flexible molecular coding and molecular evolvability.

Y Husimi1, T Aita, I Tabuchi.   

Abstract

Evolvability of biopolymers is based on molecular coding. The molecular coding is represented by biopolymer function vs monomeric sequence relationship, that is, a proper fitness landscape on the sequence space. On the other hand, molecular coding is mostly realized by monomeric sequence vs biopolymer structure relationship. We suggest the evolution of evolvability based on flexible or multiplex coding originating from flexible or polymorphic conformation of evolving biopolymers. We report a finding supporting that the amino acid landscape of the standard genetic code for an amino acid property which is more important to the protein function gives higher value of an evolvability measure. We developed a promising molecular construct which realized genotype-phenotype linking in order to study the in vitroprotein evolution to clarify above mentioned protein evolvability.

Keywords:  fitness landscape; genetic code; in vitrovirus; remote homolog proteins; sequence space

Year:  2002        PMID: 23345793      PMCID: PMC3456740          DOI: 10.1023/A:1020305815106

Source DB:  PubMed          Journal:  J Biol Phys        ISSN: 0092-0606            Impact factor:   1.365


  15 in total

1.  Junctional amino acids determine the maturation pathway of an antibody.

Authors:  K Furukawa; A Akasako-Furukawa; H Shirai; H Nakamura; T Azuma
Journal:  Immunity       Date:  1999-09       Impact factor: 31.745

2.  Analysis of a local fitness landscape with a model of the rough Mt. Fuji-type landscape: application to prolyl endopeptidase and thermolysin.

Authors:  T Aita; H Uchiyama; T Inaoka; M Nakajima; T Kokubo; Y Husimi
Journal:  Biopolymers       Date:  2000-07       Impact factor: 2.505

3.  From amino acid landscape to protein landscape: analysis of genetic codes in terms of fitness landscape.

Authors:  T Aita; S Urata; Y Husimi
Journal:  J Mol Evol       Date:  2000-04       Impact factor: 2.395

4.  One sequence, two ribozymes: implications for the emergence of new ribozyme folds.

Authors:  E A Schultes; D P Bartel
Journal:  Science       Date:  2000-07-21       Impact factor: 47.728

5.  An in vitro DNA virus for in vitro protein evolution.

Authors:  I Tabuchi; S Soramoto; N Nemoto; Y Husimi
Journal:  FEBS Lett       Date:  2001-11-23       Impact factor: 4.124

6.  cDNA - protein fusions: covalent protein - gene conjugates for the in vitro selection of peptides and proteins.

Authors:  M Kurz; K Gu; A Al-Gawari; P A Lohse
Journal:  Chembiochem       Date:  2001-09-03       Impact factor: 3.164

7.  RNA-peptide fusions for the in vitro selection of peptides and proteins.

Authors:  R W Roberts; J W Szostak
Journal:  Proc Natl Acad Sci U S A       Date:  1997-11-11       Impact factor: 11.205

8.  Structural insights into the evolution of an antibody combining site.

Authors:  G J Wedemayer; P A Patten; L H Wang; P G Schultz; R C Stevens
Journal:  Science       Date:  1997-06-13       Impact factor: 47.728

9.  In vitro virus: bonding of mRNA bearing puromycin at the 3'-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro.

Authors:  N Nemoto; E Miyamoto-Sato; Y Husimi; H Yanagawa
Journal:  FEBS Lett       Date:  1997-09-08       Impact factor: 4.124

10.  Functional proteins from a random-sequence library.

Authors:  A D Keefe; J W Szostak
Journal:  Nature       Date:  2001-04-05       Impact factor: 49.962

View more
  1 in total

1.  Multi-line split DNA synthesis: a novel combinatorial method to make high quality peptide libraries.

Authors:  Ichiro Tabuchi; Sayaka Soramoto; Shingo Ueno; Yuzuru Husimi
Journal:  BMC Biotechnol       Date:  2004-09-01       Impact factor: 2.563

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.