Enzyme-like proteins from an unselected library of designed amino acid sequences.
about
De novo proteins from designed combinatorial librariesEarly-stage folding in proteins (in silico) sequence-to-structure relation.Catalytic efficiency of designed catalytic proteinsProtein design: toward functional metalloenzymesStructure and dynamics of de novo proteins from a designed superfamily of 4-helix bundlesInstalling hydrolytic activity into a completely de novo protein frameworkProtein dynamism and evolvability.Flexible Proteins at the Origin of Life.Application of the "codon-shuffling" method. Synthesis and selection of de novo proteins as antibacterials.A promiscuous glutathione transferase transformed into a selective thiolester hydrolase.Peroxidase activity of de novo heme proteins immobilized on electrodes.Selecting folded proteins from a library of secondary structural elements.Selection and structural analysis of de novo proteins from an alpha3beta3 genetic library.Trimethyl lock: a stable chromogenic substrate for esterases.Expression, purification, and characterization of proteins from high-quality combinatorial libraries of the mammalian calmodulin central linkerComputational design and elaboration of a de novo heterotetrameric alpha-helical protein that selectively binds an emissive abiological (porphinato)zinc chromophoreBinding of small molecules to cavity forming mutants of a de novo designed protein.Small and Random Peptides: An Unexplored Reservoir of Potentially Functional Primitive Organocatalysts. The Case of Seryl-Histidine.Design, expression, and purification of de novo transmembrane "hairpin" peptides.Proteins from an unevolved library of de novo designed sequences bind a range of small molecules.Functional engineered channels and pores (Review).A de novo protein confers copper resistance in Escherichia coli.Catalysis by a de novo zinc-mediated protein interface: implications for natural enzyme evolution and rational enzyme engineering.Ligand binding and allostery can emerge simultaneously.Fast, cheap and out of control--Insights into thermodynamic and informatic constraints on natural protein sequences from de novo protein design.Design of amphiphilic protein maquettes: controlling assembly, membrane insertion, and cofactor interactionsDe novo design of catalytic proteins.Cofactor binding and enzymatic activity in an unevolved superfamily of de novo designed 4-helix bundle proteins.Incorporation of a single His residue by rational design enables thiol-ester hydrolysis by human glutathione transferase A1-1.Short peptides self-assemble to produce catalytic amyloids.Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Cascaded walks in protein sequence space: use of artificial sequences in remote homology detection between natural proteins.The effect of sequence on the conformational stability of a model heteropolymer in explicit water.The amyloid architecture provides a scaffold for enzyme-like catalysts.Experimental and theoretical study of the mechanism of hydrolysis of substituted phenyl hexanoates catalysed by globin in the presence of surfactant.
P2860
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P2860
Enzyme-like proteins from an unselected library of designed amino acid sequences.
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Enzyme-like proteins from an unselected library of designed amino acid sequences.
@ast
Enzyme-like proteins from an unselected library of designed amino acid sequences.
@en
type
label
Enzyme-like proteins from an unselected library of designed amino acid sequences.
@ast
Enzyme-like proteins from an unselected library of designed amino acid sequences.
@en
prefLabel
Enzyme-like proteins from an unselected library of designed amino acid sequences.
@ast
Enzyme-like proteins from an unselected library of designed amino acid sequences.
@en
P356
P1476
Enzyme-like proteins from an unselected library of designed amino acid sequences.
@en
P2093
Michael H Hecht
P356
10.1093/PROTEIN/GZH007
P577
2004-01-01T00:00:00Z