Investigating protein structural plasticity by surveying the consequence of an amino acid deletion from TEM-1 beta-lactamase.

Investigating protein structural plasticity by surveying the consequence of an amino acid deletion from TEM-1 beta-lactamase.

Item
http://www.wikidata.org/entity/Q30363142
Random Single Amino Acid Deletion Sampling Unveils Structural Tolerance and the Benefits of Helical Registry Shift on GFP Folding and StructureStructural and dynamic changes associated with beneficial engineered single-amino-acid deletion mutations in enhanced green fluorescent proteinRecombining low homology, functionally rich regions of bacterial subtilisins by combinatorial fragment exchangeComputational prediction of the tolerance to amino-acid deletion in green-fluorescent protein.Computed structures of point deletion mutants and their enzymatic activities.Linking the functions of unrelated proteins using a novel directed evolution domain insertion methodExpanded molecular diversity generation during directed evolution by trinucleotide exchange (TriNEx).Systematic analysis of insertions and deletions specific to nematode proteins and their proposed functional and evolutionary relevance.Extensive libraries of gene truncation variants generated by in vitro transposition.Deletion mutations conferring substrate spectrum extension in the class A β-lactamase.Generation of comprehensive transposon insertion mutant library for the model archaeon, Haloferax volcanii, and its use for gene discovery.Structural plasticity of green fluorescent protein to amino acid deletions and fluorescence rescue by folding-enhancing mutations.Natural evolution of TEM-1 β-lactamase: experimental reconstruction and clinical relevance.Functional modulation and directed assembly of an enzyme through designed non-natural post-translation modification.Studies on structure-based sequence alignment and phylogenies of beta-lactamases.Substrate spectrum extension of PenA in Burkholderia thailandensis with a single amino acid deletion, Glu168delΔFlucs: Brighter Photinus pyralis firefly luciferases identified by surveying consecutive single amino acid deletion mutations in a thermostable variant.
P2860

Investigating protein structural plasticity by surveying the consequence of an amino acid deletion from TEM-1 beta-lactamase.

Item
http://www.wikidata.org/entity/Q30363142
description
2007 nî lūn-bûn
@nan
2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Investigating protein structur ...... ion from TEM-1 beta-lactamase.
@ast
Investigating protein structur ...... ion from TEM-1 beta-lactamase.
@en
type
label
Investigating protein structur ...... ion from TEM-1 beta-lactamase.
@ast
Investigating protein structur ...... ion from TEM-1 beta-lactamase.
@en
prefLabel
Investigating protein structur ...... ion from TEM-1 beta-lactamase.
@ast
Investigating protein structur ...... ion from TEM-1 beta-lactamase.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P356
P1433
P1476
Investigating protein structur ...... ion from TEM-1 beta-lactamase.
@en
P2093
P2860
P304
P31
P356
10.1016/J.FEBSLET.2007.07.018
P407
P433
P478
P577
P5875
P698