about
In vitro Engineering of Novel Bioactivity in the Natural EnzymesISAMBARD: an open-source computational environment for biomolecular analysis, modelling and design.Smoothing a rugged protein folding landscape by sequence-based redesign.Computational tools help improve protein stability but with a solubility tradeoff.The Architecture of the Anbu Complex Reflects an Evolutionary Intermediate at the Origin of the Proteasome System.Synthetic Protein Switches: Theoretical and Experimental Considerations.Insights from molecular dynamics simulations for computational protein design.Peptide consensus sequence determination for the enhancement of the antimicrobial activity and selectivity of antimicrobial peptides.Structural and Dynamics Comparison of Thermostability in Ancient, Modern, and Consensus Elongation Factor Tus.Probing the folding pathway of a consensus serpin using single tryptophan mutants.An Engineered Glycerol Dehydratase With Improved Activity for the Conversion of meso-2,3-butanediol to Butanone.Revealing Additional Stereocomplementary Pairs of Old Yellow Enzymes by Rational Transfer of Engineered Residues.Coevolution of both thermostability and activity of polyphosphate glucokinase from YXConsensus designs and thermal stability determinants of a human glutamate transporter
P2860
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P2860
description
2016 nî lūn-bûn
@nan
2016 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
name
Consensus protein design
@ast
Consensus protein design
@en
Consensus protein design
@nl
type
label
Consensus protein design
@ast
Consensus protein design
@en
Consensus protein design
@nl
prefLabel
Consensus protein design
@ast
Consensus protein design
@en
Consensus protein design
@nl
P2860
P921
P3181
P356
P1476
Consensus protein design
@en
P2093
Benjamin T Porebski
P2860
P304
P3181
P356
10.1093/PROTEIN/GZW015
P407
P577
2016-06-05T00:00:00Z