Directed evolution of an extremely stable fluorescent protein.
about
Directed evolution of bright mutants of an oxygen-independent flavin-binding fluorescent protein from Pseudomonas putidaBeta-barrel scaffold of fluorescent proteins: folding, stability and role in chromophore formation.Separation of Escherichia coli bacteria from peripheral blood mononuclear cells using standing surface acoustic waves.Multiple global suppressors of protein stability defects facilitate the evolution of extended-spectrum TEM β-lactamases.Phanta: a non-fluorescent photochromic acceptor for pcFRET.Expression, purification, crystallization and preliminary X-ray analysis of eCGP123, an extremely stable monomeric green fluorescent protein with reversible photoswitching properties.X-Ray Crystal Structure and Properties of Phanta, a Weakly Fluorescent Photochromic GFP-Like Protein.Thermal green protein, an extremely stable, nonaggregating fluorescent protein created by structure-guided surface engineering.Novel Thermostable Flavin-binding Fluorescent Proteins from Thermophilic Organisms.Engineering and Characterization of a Fluorescent Native-Like HIV-1 Envelope Glycoprotein Trimer.Phototransformable fluorescent proteins: which one for which application?Application of the thermostable β-galactosidase, BgaB, from Geobacillus stearothermophilus as a versatile reporter under anaerobic and aerobic conditions.Properties and mutation studies of a bacteriophage-derived chimeric recombinant staphylolytic protein P128: Comparison to recombinant lysostaphin.Trade-offs between enzyme fitness and solubility illuminated by deep mutational scanning.Circularly permuted monomeric red fluorescent proteins with new termini in the beta-sheet.Engineering color variants of green fluorescent protein (GFP) for thermostability, pH-sensitivity, and improved folding kinetics.Mispacking and the Fitness Landscape of the Green Fluorescent Protein Chromophore Milieu.In vivo selection of sfGFP variants with improved and reliable functionality in industrially important thermophilic bacteria.Influence of cell surface structures on crenarchaeal biofilm formation using a thermostable green fluorescent protein.Force spectroscopy predicts thermal stability of immobilized proteins by measuring microbead mechanics.On the Potential Origins of the High Stability of Reconstructed Ancestral Proteins.Exploring new strategies for cellulosic biofuels production
P2860
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P2860
Directed evolution of an extremely stable fluorescent protein.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
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2009年学术文章
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2009年学术文章
@zh-hans
2009年学术文章
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2009年学术文章
@zh-sg
2009年學術文章
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2009年學術文章
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2009年學術文章
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name
Directed evolution of an extremely stable fluorescent protein.
@en
Directed evolution of an extremely stable fluorescent protein.
@nl
type
label
Directed evolution of an extremely stable fluorescent protein.
@en
Directed evolution of an extremely stable fluorescent protein.
@nl
prefLabel
Directed evolution of an extremely stable fluorescent protein.
@en
Directed evolution of an extremely stable fluorescent protein.
@nl
P2093
P2860
P356
P1476
Directed evolution of an extremely stable fluorescent protein
@en
P2093
Csaba Kiss
Geoffrey S Waldo
Jamshid Temirov
Leslie Chasteen
P2860
P304
P356
10.1093/PROTEIN/GZP006
P577
2009-05-01T00:00:00Z