Improvement of Bacillus circulans beta-amylase activity attained using the ancestral mutation method.
about
Exploiting models of molecular evolution to efficiently direct protein engineeringDirected evolution: an evolving and enabling synthetic biology toolDeciphering Modern Glucocorticoid Cross-pharmacology Using Ancestral Corticosteroid ReceptorsCrystal structure of β-galactosidase from Bacillus circulans ATCC 31382 (BgaD) and the construction of the thermophilic mutantsUtilizing natural diversity to evolve protein function: applications towards thermostability.Stabilizing proteins from sequence statistics: the interplay of conservation and correlation in triosephosphate isomerase stability.Assessing the prediction fidelity of ancestral reconstruction by a library approach.Modulating protein stability - directed evolution strategies for improved protein function.Expanding the metabolic engineering toolbox with directed evolution.Recent advances in rational approaches for enzyme engineering.Robust enzyme design: bioinformatic tools for improved protein stability.Characterization of Reconstructed Ancestral Proteins Suggests a Change in Temperature of the Ancient Biosphere.Ancestral amino acid substitution improves the thermal stability of recombinant lignin-peroxidase from white-rot fungi, Phanerochaete chrysosporium strain UAMH 3641.Structural and Dynamics Comparison of Thermostability in Ancient, Modern, and Consensus Elongation Factor Tus.Ancestral Haloalkane Dehalogenases Show Robustness and Unique Substrate Specificity.Discovery and Protein Engineering of Biocatalysts for Organic Synthesis
P2860
Q24635353-7B8F20F3-8FDB-4D19-AFE3-E736D6A8A0DBQ26823011-8360772C-1D91-47FA-9A01-D1AAB5918307Q27678139-CA7503D6-F905-4F25-B8EE-9E3C053E798FQ27700209-1369690A-22C4-4ABF-ADD7-6720D91F36CEQ33864392-B1F05F1D-981B-47FC-A57D-395E8F116FADQ34255270-5E6DDB25-0887-401E-81B5-8BDB34C85044Q35746785-51A01D98-2B15-4EEA-8417-C0267F2A486BQ38109676-1C248483-7A63-4708-A277-C8C45E756693Q38121854-8FC82590-F2FF-481F-B8EA-A98EE1A3A8E7Q38201023-83499D47-BEA3-4BDE-B908-4CF7227B3DDEQ38294224-0B3A1657-6301-4E63-97B8-5112A09DBE1BQ38637253-684C63E0-23F2-416A-B365-D119F61B09F2Q41094733-2C2B4CA5-2E7E-40DA-80A6-459F15D8E647Q47177793-5CF33500-61E1-4E24-8354-19E8191EB71BQ50911929-EC4359BC-33F9-490F-B424-16C2445799B9Q57189276-848C6104-E385-4087-A8B5-72A7572DF007
P2860
Improvement of Bacillus circulans beta-amylase activity attained using the ancestral mutation method.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
2010年學術文章
@zh-hant
name
Improvement of Bacillus circul ...... the ancestral mutation method.
@en
Improvement of Bacillus circul ...... the ancestral mutation method.
@nl
type
label
Improvement of Bacillus circul ...... the ancestral mutation method.
@en
Improvement of Bacillus circul ...... the ancestral mutation method.
@nl
prefLabel
Improvement of Bacillus circul ...... the ancestral mutation method.
@en
Improvement of Bacillus circul ...... the ancestral mutation method.
@nl
P2860
P356
P1476
Improvement of Bacillus circul ...... the ancestral mutation method
@en
P2093
Kan Yamashiro
Satoshi Koikeda
P2860
P304
P356
10.1093/PROTEIN/GZQ021
P577
2010-04-20T00:00:00Z