An active enzyme constructed from a 9-amino acid alphabet.
about
Directed evolution of a model primordial enzyme provides insights into the development of the genetic codeOn the evolution of the standard amino-acid alphabetThe farther, the safer: a manifesto for securely navigating synthetic species away from the old living worldCrystal structure of an extensively simplified variant of bovine pancreatic trypsin inhibitor in which over one-third of the residues are alaninesSimplification of the genetic code: restricted diversity of genetically encoded amino acidsXenomicrobiology: a roadmap for genetic code engineeringComparison of the frequency of functional SH3 domains with different limited sets of amino acids using mRNA display.Assessing side-chain perturbations of the protein backbone: a knowledge-based classification of residue Ramachandran space.Reduced alphabet for protein folding prediction.Amino acid alphabet reduction preserves fold information contained in contact interactions in proteins.Shedding light on the efficacy of laboratory evolution based on iterative saturation mutagenesis.Selection and structural analysis of de novo proteins from an alpha3beta3 genetic library.Comparative characterization of random-sequence proteins consisting of 5, 12, and 20 kinds of amino acids.Protein evolution via amino acid and codon elimination.Many pathways in laboratory evolution can lead to improved enzymes: how to escape from local minima.A metabolic prototype for eliminating tryptophan from the genetic codeAssessing directed evolution methods for the generation of biosynthetic enzymes with potential in drug biosynthesis.Improvement of biocatalysts for industrial and environmental purposes by saturation mutagenesisReconstructing a flavodoxin oxidoreductase with early amino acids.How does a simplified-sequence protein fold?The dawn of evolutionary genome engineering.Overcoming Challenges in Engineering the Genetic CodeCrystal structures of highly simplified BPTIs provide insights into hydration-driven increase of unfolding enthalpy.DNAzyme-mediated catalysis with only guanosine and cytidine nucleotides.A single aromatic core mutation converts a designed "primitive" protein from halophile to mesophile folding.Reduced alphabet motif methodology for GPCR annotation.Modern diversification of the amino acid repertoire driven by oxygen.Comprehensive reduction of amino acid set in a protein suggests the importance of prebiotic amino acids for stable proteins.Reconstruction of cysteine biosynthesis using engineered cysteine-free enzymes.Binary genetic cassettes for selecting XNA-templated DNA synthesis in vivo.Comparing Different Strategies in Directed Evolution of Enzyme Stereoselectivity: Single- versus Double-Code Saturation Mutagenesis.Simplification of complexity in protein molecular systems by grouping amino acids: a view from physicsEvaluation of 4-substituted styrenes as functional monomers for the synthesis of theophylline-specific molecularly imprinted polymers
P2860
Q21092411-0B822213-F590-471A-8FAA-AE4A5CA2A371Q21184155-E66D903D-38E8-43D2-B188-FD56A45F6ED3Q24655357-5BE22CCC-074C-47A1-8837-1E4266339881Q27652338-6DEF532B-5BF3-403A-A6EC-7293504E5579Q27671629-6066D387-FE8E-404A-944E-2E6272EF6D09Q28597532-A5F4CAB3-23C1-4462-BA0F-A7BAE73A262AQ30155604-7AE818CE-0233-4B2E-AEA3-73330C751C11Q30368561-15D95668-4035-4397-8709-EDE4809B6BD4Q30371317-45DA34B0-94A2-47D9-A56A-0D5163074351Q30379551-1C6F643A-1825-4E5C-B1A6-7CB2954E453EQ33401270-FE794C28-65B7-40D3-97C7-AB0733F7A585Q33403290-1F5FD10A-9875-4F69-BC71-327DD33925DFQ33531865-B90D60BF-DDB8-4CD1-9CDA-3EA750A6B3CFQ33570364-98016942-3E46-4BEF-9595-E8D909EEF66EQ34241242-E7F47412-1749-43B0-84BB-A16CFC6678A0Q34330197-0D6A6453-179D-4E13-B8C9-AC54BF3CEBB7Q35161643-C3E35ACE-71EC-4A0A-86C1-33D15D757144Q35196065-F2273A04-07AF-4D27-A59D-D335F06C5152Q37007440-9A79F7D3-D88C-4535-9D87-2CF56040CC70Q37359475-8CCCF76E-ABF6-496E-9AB6-D9BD174ED28CQ38215368-6267BA9B-3081-48B2-92C5-BF1B22C7A84DQ38582812-68EB78C7-A9A5-41FB-82D1-C7834623F454Q41894115-4BE22320-5B9E-485A-A54F-994EF2A9E991Q41981714-29DAC5AB-0B58-401B-B69C-1E7CCC2A3387Q43023038-8CD658E9-52F8-431E-A13C-6C29785EE162Q45965118-B7B92EAF-3056-4B97-868F-486BCA24C019Q47233749-24063099-9393-48D1-BEA1-5F44866EA182Q49179220-10726D10-C6E5-4631-BE5F-6318B508E1B3Q49572395-214FAAE7-37CD-40EF-B4FA-73DF1B47C9C1Q50875137-C64F2036-0317-4138-8947-B8BB954845F2Q51250984-C99BA421-BCA6-4569-9C22-530C98F09D19Q58159741-9E1FF753-C1E4-4CC9-8326-79A54E230048Q58200377-8C80EC06-20FB-4C40-8F4A-25B46194487E
P2860
An active enzyme constructed from a 9-amino acid alphabet.
description
2005 nî lūn-bûn
@nan
2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
An active enzyme constructed from a 9-amino acid alphabet.
@ast
An active enzyme constructed from a 9-amino acid alphabet.
@en
An active enzyme constructed from a 9-amino acid alphabet.
@nl
type
label
An active enzyme constructed from a 9-amino acid alphabet.
@ast
An active enzyme constructed from a 9-amino acid alphabet.
@en
An active enzyme constructed from a 9-amino acid alphabet.
@nl
prefLabel
An active enzyme constructed from a 9-amino acid alphabet.
@ast
An active enzyme constructed from a 9-amino acid alphabet.
@en
An active enzyme constructed from a 9-amino acid alphabet.
@nl
P2093
P2860
P356
P1476
An active enzyme constructed from a 9-amino acid alphabet.
@en
P2093
Donald Hilvert
Kai U Walter
Katherina Vamvaca
P2860
P304
37742-37746
P356
10.1074/JBC.M507210200
P407
P577
2005-09-06T00:00:00Z