Establishing wild-type levels of catalytic activity on natural and artificial ( )8-barrel protein scaffolds
about
Exploring protein fitness landscapes by directed evolutionWhy reinvent the wheel? Building new proteins based on ready-made partsMetamorphic proteins mediate evolutionary transitions of structureBisubstrate specificity in histidine/tryptophan biosynthesis isomerase from Mycobacterium tuberculosis by active site metamorphosisMolecular Engineering of Organophosphate Hydrolysis Activity from a Weak Promiscuous Lactonase TemplateA sugar isomerization reaction established on various (βα)₈-barrel scaffolds is based on substrate-assisted catalysisEstablishing catalytic activity on an artificial (βα)8-barrel protein designed from identical half-barrelsEvolutionary relationship of two ancient protein superfoldsTwo independently folding units of Plasmodium profilin suggest evolution via gene fusionDe novo design of a four-fold symmetric TIM-barrel protein with atomic-level accuracyStructural and functional innovations in the real-time evolution of new (βα)8 barrel enzymes.Functional β-propeller lectins by tandem duplications of repetitive units.A Heritable Recombination system for synthetic Darwinian evolution in yeast.Highly diverse protein library based on the ubiquitous (β/α)₈ enzyme fold yields well-structured proteins through in vitro folding selection.Assessing directed evolution methods for the generation of biosynthetic enzymes with potential in drug biosynthesis.Design of symmetric TIM barrel proteins from first principles.Related (βα)8-barrel proteins in histidine and tryptophan biosynthesis: a paradigm to study enzyme evolution.Engineering chimaeric proteins from fold fragments: 'hopeful monsters' in protein design.Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Extreme makeover: Engineering the activity of a thermostable alcohol dehydrogenase (AdhD) from Pyrococcus furiosus.De Novo Evolutionary Emergence of a Symmetrical Protein Is Shaped by Folding Constraints.Long-Term Persistence of Bi-functionality Contributes to the Robustness of Microbial Life through Exaptation.Cascaded walks in protein sequence space: use of artificial sequences in remote homology detection between natural proteins.External application of gametophyte-specific ZmPMEI1 induces pollen tube burst in maize.Frag'r'Us: knowledge-based sampling of protein backbone conformations for de novo structure-based protein design.A highly stable protein chimera built from fragments of different folds.Structure-based directed evolution of a monomeric triosephosphate isomerase: toward a pentose sugar isomerase.Highly active enzymes by automated combinatorial backbone assembly and sequence design
P2860
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P2860
Establishing wild-type levels of catalytic activity on natural and artificial ( )8-barrel protein scaffolds
description
2009 nî lūn-bûn
@nan
2009 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մարտին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Establishing wild-type levels ...... ( )8-barrel protein scaffolds
@ast
Establishing wild-type levels ...... ( )8-barrel protein scaffolds
@en
Establishing wild-type levels ...... ( )8-barrel protein scaffolds
@nl
type
label
Establishing wild-type levels ...... ( )8-barrel protein scaffolds
@ast
Establishing wild-type levels ...... ( )8-barrel protein scaffolds
@en
Establishing wild-type levels ...... ( )8-barrel protein scaffolds
@nl
prefLabel
Establishing wild-type levels ...... ( )8-barrel protein scaffolds
@ast
Establishing wild-type levels ...... ( )8-barrel protein scaffolds
@en
Establishing wild-type levels ...... ( )8-barrel protein scaffolds
@nl
P2860
P50
P356
P1476
Establishing wild-type levels ...... ( )8-barrel protein scaffolds
@en
P2860
P304
P356
10.1073/PNAS.0810342106
P407
P577
2009-03-10T00:00:00Z