Mutagenesis of a buried polar interaction in an SH3 domain: sequence conservation provides the best prediction of stability effects.
about
Native protein sequences are close to optimal for their structuresTheoretical and experimental demonstration of the importance of specific nonnative interactions in protein foldingDistinct Peptide Binding Specificities of Src Homology 3 (SH3) Protein Domains Can Be Determined by Modulation of Local Energetics across the Binding InterfaceInteraction of the Saccharomyces cerevisiae cortical actin patch protein Rvs167p with proteins involved in ER to Golgi vesicle traffickingYeast adaptor protein, Nbp2p, is conserved regulator of fungal Ptc1p phosphatases and is involved in multiple signaling pathwaysOptimization of specificity in a cellular protein interaction network by negative selection.Protein interaction domains of the ubiquitin-specific protease, USP7/HAUSPIntrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR.The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro.A residue in helical conformation in the native state adopts a β-strand conformation in the folding transition state despite its high and canonical Φ-value.Kinetic consequences of native state optimization of surface-exposed electrostatic interactions in the Fyn SH3 domain.Proline substitutions and threonine pseudophosphorylation of the SH3 ligand of 18.5-kDa myelin basic protein decrease its affinity for the Fyn-SH3 domain and alter process development and protein localization in oligodendrocytesA Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function.Comparison of the frequency of functional SH3 domains with different limited sets of amino acids using mRNA display.The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state.Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain.Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.Folding of a highly conserved diverging turn motif from the SH3 domain.The design of a hyperstable mutant of the Abp1p SH3 domain by sequence alignment analysisThe identification of conserved interactions within the SH3 domain by alignment of sequences and structures.Energetics of aliphatic deletions in protein coresStructural and dynamic properties that govern the stability of an engineered fibronectin type III domainDramatic acceleration of protein folding by stabilization of a nonnative backbone conformationProtein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins.Inferring stabilizing mutations from protein phylogenies: application to influenza hemagglutinin.Computational design of the Fyn SH3 domain with increased stability through optimization of surface charge charge interactionsThe energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopySmoothing a rugged protein folding landscape by sequence-based redesign.Increasing protein stability using a rational approach combining sequence homology and structural alignment: Stabilizing the WW domain.Translational-entropy gain of solvent upon protein folding.Linking genotype and phenotype of Saccharomyces cerevisiae strains reveals metabolic engineering targets and leads to triterpene hyper-producers.Disassembly/reassembly strategy for the production of highly pure GroEL, a tetradecameric supramolecular machine, suitable for quantitative NMR, EPR and mutational studies.The creation of a novel fluorescent protein by guided consensus engineering.Quantitative measurements of protein-surface interaction thermodynamics
P2860
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P2860
Mutagenesis of a buried polar interaction in an SH3 domain: sequence conservation provides the best prediction of stability effects.
description
1998 nî lūn-bûn
@nan
1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Mutagenesis of a buried polar ...... ediction of stability effects.
@ast
Mutagenesis of a buried polar ...... ediction of stability effects.
@en
type
label
Mutagenesis of a buried polar ...... ediction of stability effects.
@ast
Mutagenesis of a buried polar ...... ediction of stability effects.
@en
prefLabel
Mutagenesis of a buried polar ...... ediction of stability effects.
@ast
Mutagenesis of a buried polar ...... ediction of stability effects.
@en
P356
P1433
P1476
Mutagenesis of a buried polar ...... rediction of stability effects
@en
P2093
Davidson AR
P304
16172-16182
P356
10.1021/BI981788P
P407
P577
1998-11-01T00:00:00Z