Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120
about
Reversibility of biotin-binding by selective modification of tyrosine in avidinStructural elements responsible for conversion of streptavidin to a pseudoenzymeA monovalent streptavidin with a single femtomolar biotin binding siteThe origins of femtomolar protein-ligand binding: hydrogen-bond cooperativity and desolvation energetics in the biotin-(strept)avidin binding siteAvidin related protein 2 shows unique structural and functional features among the avidin protein family.Electrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomicsSer45 plays an important role in managing both the equilibrium and transition state energetics of the streptavidin-biotin systemChicken avidin exhibits pseudo-catalytic properties. Biochemical, structural, and electrostatic consequencesLigand exchange between proteins. Exchange of biotin and biotin derivatives between avidin and streptavidinTamavidins--novel avidin-like biotin-binding proteins from the Tamogitake mushroomHow the biotin–streptavidin interaction was made even stronger: investigation via crystallography and a chimaeric tetramerEvolved streptavidin mutants reveal key role of loop residue in high-affinity bindingStreptavidin and its biotin complex at atomic resolutionSecond-Contact Shell Mutation Diminishes Streptavidin–Biotin Binding Affinity through Transmitted Effects on Equilibrium DynamicsStructural consequences of cutting a binding loop: two circularly permuted variants of streptavidinStructural Adaptation of a Thermostable Biotin-binding Protein in a Psychrophilic EnvironmentDevelopment of a Tetrameric Streptavidin Mutein with Reversible Biotin Binding Capability: Engineering a Mobile Loop as an Exit Door for BiotinContamination from an affinity column: an encounter with a new villain in the world of membrane-protein crystallizationStructure-based engineering of streptavidin monomer with a reduced biotin dissociation rateMeasuring transmembrane helix interaction strengths in lipid bilayers using steric trapping.A TAT-streptavidin fusion protein directs uptake of biotinylated cargo into mammalian cells.Avidin-biotin interactions at vesicle surfaces: adsorption and binding, cross-bridge formation, and lateral interactions.The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy.Flexibility of a biotinylated ligand in artificial metalloenzymes based on streptavidin--an insight from molecular dynamics simulations with classical and ab initio force fields.Method to measure strong protein-protein interactions in lipid bilayers using a steric trap.Successful radiotherapy of tumor in pretargeted mice by 188Re-radiolabeled phosphorodiamidate morpholino oligomer, a synthetic DNA analogue.Library design and screening protocol for artificial metalloenzymes based on the biotin-streptavidin technology.Engineering subunit association of multisubunit proteins: a dimeric streptavidin.Characterization of the first fully human anti-TEM1 scFv in models of solid tumor imaging and immunotoxin-based therapy.Structural studies of the streptavidin binding loop.Melatonin attenuates hypertension-induced renal injury partially through inhibiting oxidative stress in rats.Cooperative hydrogen bond interactions in the streptavidin-biotin systemDirected evolution of streptavidin variants using in vitro compartmentalization.Limitations of Adenoviral Vector-Mediated Delivery of Gold Nanoparticles to Tumors for Hyperthermia Induction.Two-dimensional protein crystallization via metal-ion coordination by naturally occurring surface histidines.A Novel Streptavidin-luciferase Fusion Protein: Preparation, Properties and Application in Hybridization Analysis of DNA.Revisiting the streptavidin-biotin binding by using an aptamer and displacement isothermal calorimetry titration.Biotin-assisted folding of streptavidin on the yeast surface.Dual-order snapshot spectral imaging of plasmonic nanoparticles.Quantification of Small Molecule-Protein Interactions using FRET between Tryptophan and the Pacific Blue Fluorophore.
P2860
Q24534270-61466B54-0A61-4942-9F33-4516FE4F7429Q24568056-891CB047-3CFD-47C9-BD28-2B62B3DDB5ABQ24645981-060B9722-3C55-4B65-8EF0-74FE6D58659BQ24655859-794D4D20-9DAB-4E88-9D1C-647CDC1D6786Q24816540-CF60D139-61EE-4749-B90C-F210C944FDA9Q26822552-A7265454-93DB-4238-BF41-4AEA15888AEBQ27624876-CEA29C02-16D5-472E-A110-125F15899294Q27632382-CCC437AF-60BD-41BB-B799-955EC0B8CD19Q27639140-9675278C-0E92-464B-8D33-2E48171C026AQ27653625-35288065-65AE-4481-8DD6-2B925215A118Q27666604-387B9247-A914-45C5-833E-B114E1E5D424Q27667559-F53CA2C6-6405-4800-9E02-90EB5EC13B45Q27673475-13AEABDB-62E0-424E-8BCE-8D0DB7495053Q27676003-4E710985-34D6-40A6-80EE-9567A846D44FQ27678220-45D024A2-AE00-4E8E-94CD-ADECA12E871DQ27678441-FBDEE3F7-70DA-4296-835B-8D3268CCACE4Q27678752-1D1E4698-882D-442A-967B-B887CF2E3965Q27682309-D49EEF1B-E072-451B-ADA3-3EDA580E525DQ27684611-D61B65B8-156E-4BC2-89EC-2FBE4F87876AQ30357100-6B7BFAB0-DA0B-4D64-9E47-B1C66A2FFB86Q33213902-43956311-544C-4CDB-A1C0-4DB2C618091CQ34017400-719C5F2D-08FC-45A2-BA46-9819F0BCB209Q34047645-7990F539-7363-4924-BB90-A32615B763BAQ34054640-E6C9FEBD-C61F-427C-847F-28C117A18DD8Q34358811-3FB245E8-CC86-4D6C-A1DE-A0DD3427F228Q35063681-8401FACD-1ED0-4004-BE21-A848EB4B8B19Q35975143-5AC1CD79-09F4-449B-B506-B868D1D85A37Q36180294-F62BF84E-33B1-47E8-AC6E-232A09394091Q36216991-3D0F75F2-1530-4A25-A2BE-4F5F2368E5C8Q36280428-DADB0A3C-149E-4866-A197-EE983DA13D93Q36390341-63574B73-2D4C-4191-AD2F-D3D701F00E0DQ36473994-F489CC7D-538A-4FEF-8A2E-A00732050795Q37041529-1CF45E30-17E5-48E9-958C-656E53A9CF33Q37438361-422D31BA-9659-46F4-A6D2-616B17546EDEQ37609724-04529D1C-FE1E-4E20-BBF6-5E48989840BCQ38290134-228B8908-8D15-46E9-85DC-9C079E373E32Q38301537-89709F37-D57C-4240-9713-865678DDDC81Q39698691-06FB9C2E-C154-4E95-9F87-675FC7C05EF1Q40007643-13AD5DEC-EBDC-4F72-B4C4-E2CA0F403C8AQ40462367-64B5ACFE-8808-4DCE-9DCE-DE30547A61CE
P2860
Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120
description
1995 nî lūn-bûn
@nan
1995 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Site-directed mutagenesis stud ...... phan residues 79, 108, and 120
@ast
Site-directed mutagenesis stud ...... phan residues 79, 108, and 120
@en
Site-directed mutagenesis stud ...... phan residues 79, 108, and 120
@nl
type
label
Site-directed mutagenesis stud ...... phan residues 79, 108, and 120
@ast
Site-directed mutagenesis stud ...... phan residues 79, 108, and 120
@en
Site-directed mutagenesis stud ...... phan residues 79, 108, and 120
@nl
prefLabel
Site-directed mutagenesis stud ...... phan residues 79, 108, and 120
@ast
Site-directed mutagenesis stud ...... phan residues 79, 108, and 120
@en
Site-directed mutagenesis stud ...... phan residues 79, 108, and 120
@nl
P2093
P2860
P356
P1476
Site-directed mutagenesis stud ...... phan residues 79, 108, and 120
@en
P2093
P2860
P304
P356
10.1073/PNAS.92.5.1754
P407
P577
1995-02-01T00:00:00Z