Robust enzyme design: bioinformatic tools for improved protein stability.
about
A single residue substitution accounts for the significant difference in thermostability between two isoforms of human cytosolic creatine kinase.Parallel workflow manager for non-parallel bioinformatic applications to solve large-scale biological problems on a supercomputer.Prediction of amino acid positions specific for functional groups in a protein family based on local sequence similarity.Sequence and structure-based comparative analysis to assess, identify and improve the thermostability of penicillin G acylases.Study of Functional and Allosteric Sites in Protein SuperfamiliesSequence homolog-based molecular engineering for shifting the enzymatic pH optimum.Mustguseal: a Server for Multiple Structure-Guided Sequence Alignment of Protein Families.Creating an Efficient Methanol-Stable Biocatalyst by Protein and Immobilization Engineering Steps towards Efficient Biosynthesis of Biodiesel.Protein Stability: Enhancement and Measurement.Bioinformatic analysis of the fold type I PLP-dependent enzymes reveals determinants of reaction specificity in l-threonine aldolase from Aeromonas jandaei.Editorial: Protein stabilization - crossroad for protein-based processes and products
P2860
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P2860
Robust enzyme design: bioinformatic tools for improved protein stability.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
2014年论文
@zh
2014年论文
@zh-cn
name
Robust enzyme design: bioinformatic tools for improved protein stability.
@en
type
label
Robust enzyme design: bioinformatic tools for improved protein stability.
@en
prefLabel
Robust enzyme design: bioinformatic tools for improved protein stability.
@en
P2860
P356
P1476
Robust enzyme design: bioinformatic tools for improved protein stability.
@en
P2093
Dmitry Suplatov
Vytas Švedas
P2860
P304
P356
10.1002/BIOT.201400150
P577
2014-12-19T00:00:00Z