0000000000247707

AUTHOR

Patrick S. Stayton

0000-0001-6939-6371

showing 3 related works from this author

Design and construction of highly stable, protease-resistant chimeric avidins.

2005

The chicken avidin gene family consists of avidin and seven separate avidin-related genes (AVRs) 1-7. Avidin protein is a widely used biochemical tool, whereas the other family members have only recently been produced as recombinant proteins and characterized. In our previous study, AVR4 was found to be the most stable biotin binding protein thus far characterized (T(m) = 106.4 degrees C). In this study, we studied further the biotin-binding properties of AVR4. A decrease in the energy barrier between the biotin-bound and unbound state of AVR4 was observed when compared with that of avidin. The high resolution structure of AVR4 facilitated comparison of the structural details of avidin and …

Models MolecularBiotin bindingInsectaProtein familyProtein subunitRecombinant Fusion ProteinsMolecular Sequence DataBiotinBiosensing TechniquesBiologyProtein EngineeringBiochemistryProtein Structure SecondaryProtein structureAnimalsAmino Acid SequenceMolecular BiologyThermostabilityCalorimetry Differential ScanningSequence Homology Amino AcidTemperatureCell BiologyProtein engineeringAvidinRecombinant ProteinsProtein Structure TertiaryKineticsBiochemistryMicroscopy FluorescenceMutagenesisBiotinylationMutationbiology.proteinChromatography GelThermodynamicsElectrophoresis Polyacrylamide GelEndopeptidase KBaculoviridaeChickensAvidinChromatography LiquidPeptide HydrolasesProtein BindingThe Journal of biological chemistry
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Internalization of novel non-viral vector TAT-streptavidin into human cells

2007

BMC Biotechnology, 7 (1)

virusesEndocytic cyclePROTEINS + POLYPEPTIDES (BIOCHEMISTRY)02 engineering and technologyei-virusperäinen vektoriProtein EngineeringgeeniterapiaPost Transductionchemistry.chemical_compoundTHERAPIES + THERAPEUTICS (MEDICINE)Drug Delivery SystemsLääketieteen bioteknologia - Medical biotechnologyInternalizationmedia_commoninfo:eu-repo/classification/ddc/5700303 health sciencesPinocytosisNocodazoleVEKTOREN (GENETISCHE TECHNIKEN)021001 nanoscience & nanotechnologyLife sciencesCell biologyEndosomal EscapeBiotinylationGene Products tatVirusesVECTORS (GENETIC TECHNIQUES)VEKTOREN (GENETISCHE TECHNIKEN); THERAPIEN + THERAPEUTIK (MEDIZIN); PROTEINE + POLYPEPTIDE (BIOCHEMIE); VECTORS (GENETIC TECHNIQUES); THERAPIES + THERAPEUTICS (MEDICINE); PROTEINS + POLYPEPTIDES (BIOCHEMISTRY)0210 nano-technologyTHERAPIEN + THERAPEUTIK (MEDIZIN)BiotechnologyResearch ArticleStreptavidinEndosomeImmunoelectron microscopymedia_common.quotation_subjectRecombinant Fusion Proteinslcsh:BiotechnologyGenetic VectorsBiologyEndocytosis03 medical and health sciencesstreptavidiiniddc:570lcsh:TP248.13-248.65HumansEndosomal Marker030304 developmental biologyMolecular biologyEndocytic VesiclechemistryStreptavidinTATPROTEINE + POLYPEPTIDE (BIOCHEMIE)HeLa CellsBMC Biotechnology
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Dual-affinity avidin molecules

2005

A recently reported dual-chain avidin was modified further to contain two distinct, independent types of ligand-binding sites within a single polypeptide chain. Chicken avidin is normally a tetrameric glycoprotein that binds water-soluble d-biotin with extreme affinity (Kd ≈ 10−15M). Avidin is utilized in various applications and techniques in the life sciences and in the nanosciences. In a recent study, we described a novel avidin monomer-fusion chimera that joins two circularly permuted monomers into a single polypeptide chain. Two of these dual-chain avidins were observed to associate spontaneously to form a dimer equivalent to the wt tetramer. In the present study, we successfully used …

DimerBiochemistryChromatography AffinityProtein Structure Secondarychemistry.chemical_compoundBiotinAffinity chromatographyTetramerStructural BiologyAnimalsBinding siteMolecular BiologyFluorescent Dyeschemistry.chemical_classificationBinding SitesbiologyChemistryTemperatureAvidinBiochemistryBiotinylationbiology.proteinThermodynamicsGlycoproteinChickensProtein BindingAvidinProteins: Structure, Function, and Bioinformatics
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