Active barnase variants with completely random hydrophobic cores.
about
Simulating evolution by gene duplication of protein features that require multiple amino acid residuesDe novo proteins from designed combinatorial librariesSolution structure and dynamics of a de novo designed three-helix bundle proteinCysteine-free rop: A four-helix bundle core mutant has wild-type stability and structure but dramatically different unfolding kineticsA model of dynamic side-chain--side-chain interactions in the alpha-lactalbumin molten globuleReverse engineering the (beta/alpha )8 barrel fold.Patterned library analysis: a method for the quantitative assessment of hypotheses concerning the determinants of protein structure.De novo design of helical bundles as models for understanding protein folding and function.Stylus: a system for evolutionary experimentation based on a protein/proteome model with non-arbitrary functional constraintsDe novo design of the hydrophobic core of ubiquitin.Structural and dynamic properties that govern the stability of an engineered fibronectin type III domainStably folded de novo proteins from a designed combinatorial library.Combinatorial approaches to protein stability and structure.Massive sequence perturbation of a small protein.Statistical theory for protein ensembles with designed energy landscapes.A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme.Bicistronic DNA display for in vitro selection of Fab fragmentsMolecular evolution of the hyperthermophilic archaea of the Pyrococcus genus: analysis of adaptation to different environmental conditions.Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregationCombinatorial mutagenesis to restrict amino acid usage in an enzyme to a reduced setAre proteins well-packed?Breaking open a protein barrelTesting computational prediction of missense mutation phenotypes: functional characterization of 204 mutations of human cystathionine beta synthaseHistone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivoMolecular and histological characterization of primary (betaproteobacteria) and secondary (gammaproteobacteria) endosymbionts of three mealybug speciesCoarse-grained sequences for protein folding and designProgress toward the evolution of an organism with an expanded genetic code.Randomization of the entire active-site helix alpha 1 of the thiol-disulfide oxidoreductase DsbA from Escherichia coli.An in vivo selection system for homing endonuclease activity.Protein design: the choice of de novo sequences.When the Scaffold Cannot Be Ignored: The Role of the Hydrophobic Core in Ligand Binding and Specificity.From coiled coils to small globular proteins: design of a native-like three-helix bundle.Influence of the hydrophilic face on the folding ability and stability of alpha-helix bundles: relevance to the peptide catalytic activity.Use of quantitative structure-property relationships to predict the folding ability of model proteins.A new method to characterize hydrophobic organization of proteins: application to rational protein engineering of barnase.Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core.Investigation of amino acid specificity in the CydX small protein shows sequence plasticity at the functional level.7 Computational protein design and discovery
P2860
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P2860
Active barnase variants with completely random hydrophobic cores.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Active barnase variants with completely random hydrophobic cores.
@en
Active barnase variants with completely random hydrophobic cores.
@nl
type
label
Active barnase variants with completely random hydrophobic cores.
@en
Active barnase variants with completely random hydrophobic cores.
@nl
prefLabel
Active barnase variants with completely random hydrophobic cores.
@en
Active barnase variants with completely random hydrophobic cores.
@nl
P2860
P356
P1476
Active barnase variants with completely random hydrophobic cores.
@en
P2093
P2860
P304
P356
10.1073/PNAS.93.11.5590
P407
P50
P577
1996-05-01T00:00:00Z