Improving the thermostability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis. - Wikidata - awgldk - TriplyDB

Improving the thermostability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis.

Improving the thermostability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis.

http://www.wikidata.org/entity/Q34443628

about

HotSpot Wizard 2.0: automated design of site-specific mutations and smart libraries in protein engineering.Improvement of biocatalysts for industrial and environmental purposes by saturation mutagenesis Molecular engineering of industrial enzymes: recent advances and future prospects.Robust enzyme design: bioinformatic tools for improved protein stability.Correlated positions in protein evolution and engineering.Co-evolution techniques are reshaping the way we do structural bioinformatics.Methods and Applications of CRISPR-Mediated Base Editing in Eukaryotic Genomes.

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P2860

Improving the thermostability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis.

http://www.wikidata.org/entity/Q34443628

description

2012 nî lūn-bûn

@nan

2012 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年学术文章

@wuu

2012年学术文章

@zh-cn

2012年学术文章

@zh-hans

2012年学术文章

@zh-my

2012年学术文章

@zh-sg

2012年學術文章

@yue

name

Improving the thermostability ...... g-site saturation mutagenesis.

@ast

Improving the thermostability ...... g-site saturation mutagenesis.

@en

Improving the thermostability ...... g-site saturation mutagenesis.

@nl

type

label

Improving the thermostability ...... g-site saturation mutagenesis.

@ast

Improving the thermostability ...... g-site saturation mutagenesis.

@en

Improving the thermostability ...... g-site saturation mutagenesis.

@nl

prefLabel

Improving the thermostability ...... g-site saturation mutagenesis.

@ast

Improving the thermostability ...... g-site saturation mutagenesis.

@en

Improving the thermostability ...... g-site saturation mutagenesis.

@nl

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P356

1471-2105-13-263

P1433

BMC Bioinformatics

P1476

Improving the thermostability ...... g-site saturation mutagenesis.

@en

P2093

Bingfang He

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

Chenghua Wang

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

Qishi Du

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

Ribo Huang

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

P2860

Directed evolution drives the next generation of biocatalysts

MAFFT version 5: improvement in accuracy of multiple sequence alignment

UniProt: the Universal Protein knowledgebase

Correlated mutations and residue contacts in proteins

Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface

Stability for function trade-offs in the enolase superfamily "catalytic module"

Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes

Evolutionarily conserved pathways of energetic connectivity in protein families

Coevolving protein residues: maximum likelihood identification and relationship to structure.

Genomic biodiversity, phylogenetics and coevolution in proteins

P2888

1471-2105-13-263

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scholarly article

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10.1186/1471-2105-13-263

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13

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