Directed evolution of streptavidin variants using in vitro compartmentalization. - Wikidata - awgldk - TriplyDB

Directed evolution of streptavidin variants using in vitro compartmentalization.

Directed evolution of streptavidin variants using in vitro compartmentalization.

http://www.wikidata.org/entity/Q37041529

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A streptavidin variant with slower biotin dissociation and increased mechanostability How the biotin–streptavidin interaction was made even stronger: investigation via crystallography and a chimaeric tetramer Evolved streptavidin mutants reveal key role of loop residue in high-affinity binding A Robust and Versatile Method of Combinatorial Chemical Synthesis of Gene Libraries via Hierarchical Assembly of Partially Randomized Modules An efficient method to assemble linear DNA templates for in vitro screening and selection systems Directed evolution of the substrate specificity of biotin ligase.DNA nanoswitches: a quantitative platform for gel-based biomolecular interaction analysis Cell-free synthetic biology: thinking outside the cell.An in vitro compartmentalization-based method for the selection of bond-forming enzymes from large libraries Protein Synthesis in Sub-Micrometer Water-in-Oil Droplets.A Concept for Selection of Codon-Suppressor tRNAs Based on Read-Through Ribosome Display in an In Vitro Compartmentalized Cell-Free Translation System.

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Directed evolution of streptavidin variants using in vitro compartmentalization.

http://www.wikidata.org/entity/Q37041529

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on September 2008

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Directed evolution of streptavidin variants using in vitro compartmentalization.

@en

Directed evolution of streptavidin variants using in vitro compartmentalization.

@nl

type

label

Directed evolution of streptavidin variants using in vitro compartmentalization.

@en

Directed evolution of streptavidin variants using in vitro compartmentalization.

@nl

prefLabel

Directed evolution of streptavidin variants using in vitro compartmentalization.

@en

Directed evolution of streptavidin variants using in vitro compartmentalization.

@nl

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P356

J.CHEMBIOL.2008.07.017

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Chemistry and Biology

P1476

Directed evolution of streptavidin variants using in vitro compartmentalization.

@en

P2093

Andrew D Ellington

http://www.w3.org/2001/XMLSchema#string

Matthew Levy

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P2860

Making artificial antibodies: a format for phage display of combinatorial heterodimeric arrays

In vitro selection and evolution of functional proteins by using ribosome display

The origins of femtomolar protein-ligand binding: hydrogen-bond cooperativity and desolvation energetics in the biotin-(strept)avidin binding site

Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site

Structural studies of hydrogen bonds in the high-affinity streptavidin-biotin complex: mutations of amino acids interacting with the ureido oxygen of biotin

Structural origins of high-affinity biotin binding to streptavidin

Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex

A DNA-fuelled molecular machine made of DNA

DNA-templated self-assembly of protein arrays and highly conductive nanowires

Rapid evolution of a protein in vitro by DNA shuffling

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979-989

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scholarly article

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10.1016/J.CHEMBIOL.2008.07.017

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9

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15

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2008-09-01T00:00:00Z

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23269149

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18804035

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directed evolution

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2615486

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