Mutating the charged residues in the binding pocket of cellular retinoic acid-binding protein simultaneously reduces its binding affinity to retinoic acid and increases its thermostability.
about
Specificity determinants for lipids bound to beta-barrel proteinsA relationship between protein stability and protein functionBiochemical and crystallographic analyses of a portal mutant of the adipocyte lipid-binding proteinStructure-function relationships of cellular retinoic acid-binding proteins. Quantitative analysis of the ligand binding properties of the wild-type proteins and site-directed mutantsLipocalin-type prostaglandin D synthase (beta-trace) is a newly recognized type of retinoid transporterThe Role of Aromatic-Aromatic Interactions in Strand-Strand Stabilization of β-SheetsEmpirical relationships between protein structure and carboxyl pKa values in proteins.Common physical basis of macromolecule-binding sites in proteinsRelating destabilizing regions to known functional sites in proteins.Prediction of functional sites based on the fuzzy oil drop modelSite-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteineChapter 3: A fluorescent window into protein folding and aggregation in cellsEffect of salt on the formation of salt-bridges in β-hairpin peptides.Functional Constraint Profiling of a Viral Protein Reveals Discordance of Evolutionary Conservation and FunctionalityMonitoring protein stability and aggregation in vivo by real-time fluorescent labelingMolecular cloning and characterization of an invertebrate cellular retinoic acid binding protein.Transporter-to-trap conversion: a disulfide bond formation in cellular retinoic acid binding protein I mutant triggered by retinoic acid binding irreversibly locks the ligand inside the protein.Cross-strand split tetra-Cys motifs as structure sensors in a beta-sheet protein.Arginine 132 of cellular retinoic acid-binding protein (type II) is important for binding of retinoic acid.Ligand binding properties of human cellular retinoic acid binding protein II expressed in E. coli as a glutathione-S-transferase fusion protein.Cellular retinaldehyde-binding protein ligand interactions. Gln-210 and Lys-221 are in the retinoid binding pocket.Intrinsic tryptophans of CRABPI as probes of structure and folding.Folding of intracellular retinol and retinoic acid binding proteins.Indirect assessment of small hydrophobic ligand binding to a model protein using a combination of ESI MS and HDX/ESI MS.Transient structural disorder as a facilitator of protein-ligand binding: native H/D exchange-mass spectrometry study of cellular retinoic acid binding protein I.Stability strengths and weaknesses in protein structures detected by statistical potentials: Application to bovine seminal ribonuclease.
P2860
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P2860
Mutating the charged residues in the binding pocket of cellular retinoic acid-binding protein simultaneously reduces its binding affinity to retinoic acid and increases its thermostability.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh
1992年學術文章
@zh-hant
name
Mutating the charged residues ...... increases its thermostability.
@en
type
label
Mutating the charged residues ...... increases its thermostability.
@en
prefLabel
Mutating the charged residues ...... increases its thermostability.
@en
P2093
P356
P1433
P1476
Mutating the charged residues ...... increases its thermostability.
@en
P2093
P356
10.1002/PROT.340130202
P407
P577
1992-04-01T00:00:00Z